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Conserved domains on  [gi|1937404779|ref|WP_195942821|]
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MULTISPECIES: sugar ABC transporter substrate-binding protein [Bifidobacterium]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194401)

ABC transporter substrate-binding protein functions as the initial receptor in the active transport of one or more from a variety of substrates including sugars and contains type 2 periplasmic binding fold

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-415 5.65e-76

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


:

Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 241.16  E-value: 5.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWD-----DEMQP-IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDD 113
Cdd:cd13585     1 TLTFWDWGqpaetAALKKlIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 114 KLKDLGIDKsDFQPAVTDITNQVDGYYGFPQGFATEIMYYNKDMFDAAGvAYPTDDWTWDDYTAAAEKLTKADGSQYG-- 191
Cdd:cd13585    81 YIEKDGLDD-DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGQYGfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 192 -SDSPTFNGVWYSLIGAAGDKVVD--NGKLSFGN-GLKKTLEFQKNLVDNKWQPQPAS--GSKVSDMFAAGKAAMTLGGT 265
Cdd:cd13585   159 lRGGSGGQTQWYPFLWSNGGDLLDedDGKATLNSpEAVEALQFYVDLYKDGVAPSSATtgGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 266 WLVSTYKD--VDFKWDIATIPTAPGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMA 343
Cdd:cd13585   239 WALGTLKDskVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAAS 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937404779 344 DGYYKvqgkngPSNWSSLEASAKEAKLGYTLVASTPTFNLYDQFNAYVlgQTSLSEVTGTQVAKANKEITDA 415
Cdd:cd13585   319 AAAPD------AKPALALAAAADALAAAVPPPVPPPWPEVYPILSEAL--QEALLGALGKSPEEALKEAAKE 382
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-415 5.65e-76

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 241.16  E-value: 5.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWD-----DEMQP-IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDD 113
Cdd:cd13585     1 TLTFWDWGqpaetAALKKlIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 114 KLKDLGIDKsDFQPAVTDITNQVDGYYGFPQGFATEIMYYNKDMFDAAGvAYPTDDWTWDDYTAAAEKLTKADGSQYG-- 191
Cdd:cd13585    81 YIEKDGLDD-DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGQYGfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 192 -SDSPTFNGVWYSLIGAAGDKVVD--NGKLSFGN-GLKKTLEFQKNLVDNKWQPQPAS--GSKVSDMFAAGKAAMTLGGT 265
Cdd:cd13585   159 lRGGSGGQTQWYPFLWSNGGDLLDedDGKATLNSpEAVEALQFYVDLYKDGVAPSSATtgGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 266 WLVSTYKD--VDFKWDIATIPTAPGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMA 343
Cdd:cd13585   239 WALGTLKDskVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAAS 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937404779 344 DGYYKvqgkngPSNWSSLEASAKEAKLGYTLVASTPTFNLYDQFNAYVlgQTSLSEVTGTQVAKANKEITDA 415
Cdd:cd13585   319 AAAPD------AKPALALAAAADALAAAVPPPVPPPWPEVYPILSEAL--QEALLGALGKSPEEALKEAAKE 382
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 10-345 2.08e-75

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 238.79  E-value: 2.08e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  10 MRLVAGVAAVATLMGTAACGSSNSSSSDDN---TLTVSYWDDEMQP-----IKDFIKANPDIKVKQIRVPGDDYNTKLNQ 81
Cdd:COG1653     1 MRRLALALAAALALALAACGGGGSGAAAAAgkvTLTVWHTGGGEAAalealIKEFEAEHPGIKVEVESVPYDDYRTKLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  82 MIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDLGIDKSDFQPAVTDiTNQVDG-YYGFPQGFATEIMYYNKDMFDA 160
Cdd:COG1653    81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALD-AGTYDGkLYGVPFNTDTLGLYYNKDLFEK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 161 AGVAYPtddWTWDDYTAAAEKLTKADGsQYG-SDSPTFNGVWYSLIGAAGDKVVD-NGKLSFGN-GLKKTLEFQKNLVDN 237
Cdd:COG1653   160 AGLDPP---KTWDELLAAAKKLKAKDG-VYGfALGGKDGAAWLDLLLSAGGDLYDeDGKPAFDSpEAVEALEFLKDLVKD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 238 KWQPQPASGSKVSD---MFAAGKAAMTLGGTWLVSTYKD--VDFKWDIATIPTAPGAKKYNS-LHTSFWAINAKTKHSAA 311
Cdd:COG1653   236 GYVPPGALGTDWDDaraAFASGKAAMMINGSWALGALKDaaPDFDVGVAPLPGGPGGKKPASvLGGSGLAIPKGSKNPEA 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1937404779 312 AEKLVKFLMSKEGQKSMsqslgntPAFQSMMADG 345
Cdd:COG1653   316 AWKFLKFLTSPEAQAKW-------DALQAVLLGQ 342
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 53-348 2.36e-32

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 123.67  E-value: 2.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  53 IKDFIKANpDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADY--VRFAKNGVTMKLDDklkdlgIDKSDFQPAVT 130
Cdd:pfam13416   3 AKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIAADqlATLAEAGLLADLSD------VDNLDDLPDAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 131 DiTNQVDG-YYGFPqgFATE---IMYYNKDMFDAAGvaypTDDWTWDDYTAAAEKLTKADGSqygSDSPTFNGVWYSLig 206
Cdd:pfam13416  76 D-AAGYDGkLYGVP--YAAStptVLYYNKDLLKKAG----EDPKTWDELLAAAAKLKGKTGL---TDPATGWLLWALL-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 207 AAGDKVVDNGKlsFGNGLKKTLEFQKNLVDNKwqPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIPTA 286
Cdd:pfam13416 144 ADGVDLTDDGK--GVEALDEALAYLKKLKDNG--KVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDG 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937404779 287 PgakkynSLHTSFWAINAKTKHS-AAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMADGYYK 348
Cdd:pfam13416 220 S------FLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVK 276
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
63-288 6.10e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 41.92  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  63 IKVKqIRVPgDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNG------VTMKLDDKLKDLGIDksdfqpAVTditnqV 136
Cdd:PRK09474   59 IKVT-VEHP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGllaevtPSKAFKDKLVPFTWD------AVR-----Y 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 137 DG-YYGFPQGFATEIMYYNKDMFdaagvayPTDDWTWDDYTAAAEKLtKADGSQ---YGSDSPTFNgvwYSLIGAAGDKV 212
Cdd:PRK09474  126 NGkLIGYPIAVEALSLIYNKDLV-------PTPPKTWEEIPALDKEL-KAKGKSaimWNLQEPYFT---WPLIAADGGYA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 213 --VDNGKLSFGN------GLKKTLEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIP 284
Cdd:PRK09474  195 fkFENGGYDVKDvgvnnaGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINYGVTVLP 274


                  ....
gi 1937404779 285 TAPG 288
Cdd:PRK09474  275 TFNG 278
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-415 5.65e-76

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 241.16  E-value: 5.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWD-----DEMQP-IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDD 113
Cdd:cd13585     1 TLTFWDWGqpaetAALKKlIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 114 KLKDLGIDKsDFQPAVTDITNQVDGYYGFPQGFATEIMYYNKDMFDAAGvAYPTDDWTWDDYTAAAEKLTKADGSQYG-- 191
Cdd:cd13585    81 YIEKDGLDD-DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGQYGfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 192 -SDSPTFNGVWYSLIGAAGDKVVD--NGKLSFGN-GLKKTLEFQKNLVDNKWQPQPAS--GSKVSDMFAAGKAAMTLGGT 265
Cdd:cd13585   159 lRGGSGGQTQWYPFLWSNGGDLLDedDGKATLNSpEAVEALQFYVDLYKDGVAPSSATtgGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 266 WLVSTYKD--VDFKWDIATIPTAPGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMA 343
Cdd:cd13585   239 WALGTLKDskVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAAS 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937404779 344 DGYYKvqgkngPSNWSSLEASAKEAKLGYTLVASTPTFNLYDQFNAYVlgQTSLSEVTGTQVAKANKEITDA 415
Cdd:cd13585   319 AAAPD------AKPALALAAAADALAAAVPPPVPPPWPEVYPILSEAL--QEALLGALGKSPEEALKEAAKE 382
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 10-345 2.08e-75

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 238.79  E-value: 2.08e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  10 MRLVAGVAAVATLMGTAACGSSNSSSSDDN---TLTVSYWDDEMQP-----IKDFIKANPDIKVKQIRVPGDDYNTKLNQ 81
Cdd:COG1653     1 MRRLALALAAALALALAACGGGGSGAAAAAgkvTLTVWHTGGGEAAalealIKEFEAEHPGIKVEVESVPYDDYRTKLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  82 MIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDLGIDKSDFQPAVTDiTNQVDG-YYGFPQGFATEIMYYNKDMFDA 160
Cdd:COG1653    81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALD-AGTYDGkLYGVPFNTDTLGLYYNKDLFEK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 161 AGVAYPtddWTWDDYTAAAEKLTKADGsQYG-SDSPTFNGVWYSLIGAAGDKVVD-NGKLSFGN-GLKKTLEFQKNLVDN 237
Cdd:COG1653   160 AGLDPP---KTWDELLAAAKKLKAKDG-VYGfALGGKDGAAWLDLLLSAGGDLYDeDGKPAFDSpEAVEALEFLKDLVKD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 238 KWQPQPASGSKVSD---MFAAGKAAMTLGGTWLVSTYKD--VDFKWDIATIPTAPGAKKYNS-LHTSFWAINAKTKHSAA 311
Cdd:COG1653   236 GYVPPGALGTDWDDaraAFASGKAAMMINGSWALGALKDaaPDFDVGVAPLPGGPGGKKPASvLGGSGLAIPKGSKNPEA 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1937404779 312 AEKLVKFLMSKEGQKSMsqslgntPAFQSMMADG 345
Cdd:COG1653   316 AWKFLKFLTSPEAQAKW-------DALQAVLLGQ 342
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 53-340 2.49e-58

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 195.20  E-value: 2.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  53 IKDFIKANPDIKVKQIRVPGDDYN-TKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDLGIDKSDFQPAVTD 131
Cdd:cd14748    20 VDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDKDGVDDDDFYPAALD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 132 iTNQVDG-YYGFPQGFATEIMYYNKDMFDAAGVAYPTDDWTWDDYTAAAEKLTKADG--SQYG--SDSPTFNGVWYSLIG 206
Cdd:cd14748   100 -AGTYDGkLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGktGRYGfaLPPGDGGWTFQALLW 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 207 AAGDKVVD--NGKLSFGN-GLKKTLEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDV--DFKWDIA 281
Cdd:cd14748   179 QNGGDLLDedGGKVTFNSpEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDKgaGFEYGVA 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 282 TIPTAPGAKKYNSLHTSFWAINAK-TKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQS 340
Cdd:cd14748   259 PLPAGKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKS 318
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
6-344 3.24e-50

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 174.75  E-value: 3.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779   6 KRTVMRLVAGVAAVATLMgtAACGSSNSSSSDDN------TLTVSYWDDEMQPIKDFIKA---NPDIKVKQIRVPGDDYN 76
Cdd:COG2182     2 KRRLLAALALALALALAL--AACGSGSSSSGSSSaagaggTLTVWVDDDEAEALEEAAAAfeeEPGIKVKVVEVPWDDLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  77 TKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDlgidKSDFQPAVTDiTNQVDG-YYGFPQGFATEIMYYNK 155
Cdd:COG2182    80 EKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLAD----KDDFLPAALD-AVTYDGkLYGVPYAVETLALYYNK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 156 DMFDAAGVAyptddwTWDDYTAAAEKLTKAD--GSQYGSDSPTFngvWYSLIGAAGDKVV-----DNGKLSFGN-GLKKT 227
Cdd:COG2182   155 DLVKAEPPK------TWDELIAAAKKLTAAGkyGLAYDAGDAYY---FYPFLAAFGGYLFgkdgdDPKDVGLNSpGAVAA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 228 LEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKD-VDFKWDIATIPTAPGAKKYNS-LHTSFWAINAK 305
Cdd:COG2182   226 LEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKaLGIDYGVAPLPTLAGGKPAKPfVGVKGFGVSAY 305

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1937404779 306 TKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMAD 344
Cdd:COG2182   306 SKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAED 344
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 40-346 8.85e-50

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 172.88  E-value: 8.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTV-----SYWDDEMQPI-KDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDD 113
Cdd:cd14747     1 TLTVwamgnSAEAELLKELaDEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 114 KLKDLGIDKSDFQPAVTdiTNQVDG-YYGFPQGFATEIMYYNKDMFDAAG-VAYPTddwTWDDYTAAAEKLTKADGSQYG 191
Cdd:cd14747    81 YLEDLGGDKDLFPGLVD--TGTVDGkYYGVPWYADTRALFYRTDLLKKAGgDEAPK---TWDELEAAAKKIKADGPDVSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 192 SDSPTFNGVWYSLI----GAAGDKVVDNGKLSFGN--GLKKTLEFQKNLVDNKWQP--QPASGSKVSDMFAAGKAAMTLG 263
Cdd:cd14747   156 FAIPGKNDVWHNALpfvwGAGGDLATKDKWKATLDspEAVAGLEFYTSLYQKGLSPksTLENSADVEQAFANGKVAMIIS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 264 GTWLVSTYKD----VDFKWDIATIPTAPGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQ 339
Cdd:cd14747   236 GPWEIGAIREagpdLAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANT 315


                  ....*..
gi 1937404779 340 SMMADGY 346
Cdd:cd14747   316 SAWDDPS 322
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 42-348 1.32e-45

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 161.78  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  42 TVSYWD----DEMQP-----IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVM-LTQEADYVRFAKNGVTMKL 111
Cdd:cd14749     1 TITYWQyftgDTKKKymdelIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 112 DDKLKDLGIDKsDFQPAVTDITNQVDGYYGFPQGFATEIMYYNKDMFDAAG-VAYPTddwTWDDYTAAAEKLTKADGSQY 190
Cdd:cd14749    81 TDYLDPNGVDK-RFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPK---TWDELIEAAKKDKFKAKGQT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 191 GSDSPTFN--GVWYS---LIGAAGDKVVDN--GKLSFGN-GLKKTLEFQKNLVDNKWQPQPASGSKVSD---MFAAGKAA 259
Cdd:cd14749   157 GFGLLLGAqgGHWYFqylVRQAGGGPLSDDgsGKATFNDpAFVQALQKLQDLVKAGAFQEGFEGIDYDDagqAFAQGKAA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 260 MTLGGTWLVSTYKD--VDFKWDIATIPTAPGAKKYNSLHTSFWA--INAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNT 335
Cdd:cd14749   237 MNIGGSWDLGAIKAgePGGKIGVFPFPTVGKGAQTSTIGGSDWAiaISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLL 316

                         330
                  ....*....|...
gi 1937404779 336 PAFQSMMADGYYK 348
Cdd:cd14749   317 PAKEVVAKDEDPD 329
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 51-337 2.62e-36

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 136.66  E-value: 2.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  51 QPIKDFIKANPDIKVKQIRVPG--DDYNTKLNQ-MIVGGTAPDVMLTqeaDYV---RFAKNGVTMKLDDKLKDLGIDksD 124
Cdd:cd14750    18 KAIAAFEKKHPDIKVEIEELPAssDDQRQQLVTaLAAGSSAPDVLGL---DVIwipEFAEAGWLLPLTEYLKEEEDD--D 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 125 FQPAVTDiTNQVDG-YYGFPQGFATEIMYYNKDMFDAAGVAYPTddwTWDDYTAAAEKLTKADGSQYGsdsptFNGVWYS 203
Cdd:cd14750    93 FLPATVE-ANTYDGkLYALPWFTDAGLLYYRKDLLEKYGPEPPK---TWDELLEAAKKRKAGEPGIWG-----YVFQGKQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 204 ----------LIGAAGDKVVDN--GKLSFGN-GLKKTLEFQKNLVDNKWQPQPASGSK---VSDMFAAGKAAMTLGGTWL 267
Cdd:cd14750   164 yeglvcnfleLLWSNGGDIFDDdsGKVTVDSpEALEALQFLRDLIGEGISPKGVLTYGeeeARAAFQAGKAAFMRNWPYA 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937404779 268 VSTYKD----VDFKWDIATIPTAPGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPA 337
Cdd:cd14750   244 YALLQGpesaVAGKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPPT 317
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 40-337 5.77e-34

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 130.11  E-value: 5.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWDDE----MQPIKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKL 115
Cdd:cd13586     1 TITVWTDEDGeleyLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 116 KDLGIDKSDFQPAVTditnqVDG-YYGFPQGFATEIMYYNKDMFdaagvayPTDDWTWDDYTAAAEKLTKADGSQYGSDS 194
Cdd:cd13586    81 AVKIKNLPVALAAVT-----YNGkLYGVPVSVETIALFYNKDLV-------PEPPKTWEELIALAKKFNDKAGGKYGFAY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 195 PTFNG-VWYSLIGAAGDKV-----VDNGKLSFGN-GLKKTLEFQKNLVD-NKWQPQPASGSKVSDMFAAGKAAMTLGGTW 266
Cdd:cd13586   149 DQTNPyFSYPFLAAFGGYVfgengGDPTDIGLNNeGAVKGLKFIKDLKKkYKVLPPDLDYDIADALFKEGKAAMIINGPW 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937404779 267 LVSTYKDVDFKWDIATIPTAPGAKKYNSLHTS-FWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPA 337
Cdd:cd13586   229 DLADYKDAGINFGVAPLPTLPGGKQAAPFVGVqGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPA 300
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 53-348 2.36e-32

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 123.67  E-value: 2.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  53 IKDFIKANpDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADY--VRFAKNGVTMKLDDklkdlgIDKSDFQPAVT 130
Cdd:pfam13416   3 AKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIAADqlATLAEAGLLADLSD------VDNLDDLPDAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 131 DiTNQVDG-YYGFPqgFATE---IMYYNKDMFDAAGvaypTDDWTWDDYTAAAEKLTKADGSqygSDSPTFNGVWYSLig 206
Cdd:pfam13416  76 D-AAGYDGkLYGVP--YAAStptVLYYNKDLLKKAG----EDPKTWDELLAAAAKLKGKTGL---TDPATGWLLWALL-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 207 AAGDKVVDNGKlsFGNGLKKTLEFQKNLVDNKwqPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIPTA 286
Cdd:pfam13416 144 ADGVDLTDDGK--GVEALDEALAYLKKLKDNG--KVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDG 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937404779 287 PgakkynSLHTSFWAINAKTKHS-AAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMADGYYK 348
Cdd:pfam13416 220 S------FLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVK 276
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 42-340 3.68e-31

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 122.49  E-value: 3.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  42 TVSYWD---DEMQP-----IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDD 113
Cdd:cd14751     1 TITFWHtssDEEKVlyeklIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 114 KLKDLgiDKSDFQPAVTDiTNQVDG-YYGFPQGFATEIMYYNKDMFDAAGVAYPTddwTWDDYTAAAEKLTKADGsQYGS 192
Cdd:cd14751    81 TPAFD--DIVDYLPGPME-TNRYNGhYYGVPQVTNTLALFYNKRLLEEAGTEVPK---TMDELVAAAKAIKKKKG-RYGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 193 DSPTFNGvWYSL--IGAAGDKVVDNGKLSF---GNGLKKTLEFQKNLVDNKWQPQPASGSKVS--DMFAAGKAAMTLGGT 265
Cdd:cd14751   154 YISGDGP-YWLLpfLWSFGGDLTDEKKATGylnSPESVRALETIVDLYDEGAITPCASGGYPNmqDGFKSGRYAMIVNGP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 266 WLVSTYK-----DVDFKWDIATIPTAP-GAKKYNSLHTsfWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQ 339
Cdd:cd14751   233 WAYADILggkefKDPDNLGIAPVPAGPgGSGSPVGGED--LVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRT 310


                  .
gi 1937404779 340 S 340
Cdd:cd14751   311 S 311
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 50-326 1.60e-29

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 116.36  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  50 MQPIKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAP-DVMLTQEADYVRFAKNGVTMKLDDKLKDLGIDKsdfqpa 128
Cdd:pfam01547  11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLG------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 129 vtditnqVDGYYGFPQGFATEIMYYNKDMFDAAGVAYPtddWTWDDYTAAAEKLTKADGS---QYGSDSPTFNGVWYSLI 205
Cdd:pfam01547  85 -------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGKSpggAGGGDASGTLGYFTLAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 206 --GAAGDKVVDNGKLSFGNGLKKTLEFQKNLVDNK--------WQPQPASGSKVSDMFAAGKAAMTLGGTW--------- 266
Cdd:pfam01547 155 laSLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVlllkklknPGVAGADGREALALFEQGKAAMGIVGPWaalaankvk 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937404779 267 ----LVSTYKDVDFKWDIATIPTAPGAKKYnslhTSFWAINAKTKHSAAAEKLVKFLMSKEGQK 326
Cdd:pfam01547 235 lkvaFAAPAPDPKGDVGYAPLPAGKGGKGG----GYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 53-337 6.27e-25

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 104.80  E-value: 6.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  53 IKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDLGIDKSDFQPAVtdi 132
Cdd:cd13522    20 IAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSKSGKYAPNTIAAM--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 133 tnQVDG-YYGFPQGFATEIMYYNKDMFDaagvayPTDDWTWDDYTAAAEKLTKADGS--QYGSDSPTFngvWYSLIGAAG 209
Cdd:cd13522    97 --KLNGkLYGVPVSVGAHLMYYNKKLVP------KNPPKTWQELIALAQGLKAKNVWglVYNQNEPYF---FAAWIGGFG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 210 DKVV--DNGKLSFG---NGLKKTLEFQKNLVD-NKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVD-FKWDIAT 282
Cdd:cd13522   166 GQVFkaNNGKNNPTldtPGAVEALQFLVDLKSkYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQALkINLGVAP 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937404779 283 IPTAPGAKKYNSLHTSF-WAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPA 337
Cdd:cd13522   246 LPTFSGTKHAAPFVGGKgFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPA 301
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 54-371 1.02e-24

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 104.49  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  54 KDFIKANpDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLtqeADYVRFAKNGVTMKLDDkLKDLGIDKSDFQPAVTDIT 133
Cdd:cd13658    20 KQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMV---APHDRIGSAVLQGLLSP-IKLSKDKKKGFTDQALKAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 134 NQVDGYYGFPQGFATEIMYYNKDMFDAAgvayPTddwTWDDYTAAAEKLTKADGSQYG--SDSPTFNGVwYSLIGAAGDK 211
Cdd:cd13658    95 TYDGKLYGLPAAVETLALYYNKDLVKNA----PK---TFDELEALAKDLTKEKGKQYGflADATNFYYS-YGLLAGNGGY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 212 VV-DNGKLSFGN-------GLKKTLEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATI 283
Cdd:cd13658   167 IFkKNGSDLDINdiglnspGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVNYGVAPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 284 PTAPGAKKYNS-LHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMADGyykvQGKNGPsnwsSLE 362
Cdd:cd13658   247 PTLPNGKPMAPfLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDP----EIKNNP----LTS 318


                  ....*....
gi 1937404779 363 ASAKEAKLG 371
Cdd:cd13658   319 AFAKQASRA 327
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-416 1.02e-24

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 105.49  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWDDEMQ-------PIKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQEADYVR-FAKNGVTMKL 111
Cdd:cd13580     4 TITIVANLGGNPkpdpddnPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSItLVKQGALWDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 112 DDKLKDLGIDKSDFQPAVTDITNQVDG-YYGFPQ---GFATEIMYYNKDMFDAAGVAYPTddwTWDDYTAAAEKLTKADG 187
Cdd:cd13580    84 TDYLDKYYPNLKKIIEQEGWDSASVDGkIYGIPRkrpLIGRNGLWIRKDWLDKLGLEVPK---TLDELYEVAKAFTEKDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 188 SQYG--------SDSPTFNGVWYSLIGAAGD-----KVVDNGKLSFG---NGLKKTLEFQKNLVDNKW-QPQPA--SGSK 248
Cdd:cd13580   161 DGNGkkdtygltDTKDLIGSGFTGLFGAFGAppnnwWKDEDGKLVPGsiqPEMKEALKFLKKLYKEGLiDPEFAvnDGTK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 249 VSDMFAAGKAAMTLGGTWLVSTY------KDVDFKWDIATIPTAPGAKKY---NSLHTSFWAINAKTKHSAAAEKLVKFL 319
Cdd:cd13580   241 ANEKFISGKAGIFVGNWWDPAWPqaslkkNDPDAEWVAVPIPSGPDGKYGvwaESGVNGFFVIPKKSKKPEAILKLLDFL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 320 MSKEGQKSMSQSLGNT--------------PAFQSMMADGYYKVQGKNGPSNWsSLEASAKEAKLGYTLVASTPTFNLYD 385
Cdd:cd13580   321 SDPEVQKLLDYGIEGVhytvkdggpvniipPDKQEVGDATLDYFQGSLALEKY-KLTNNGERKSDAKKEALDERVVNAND 399

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1937404779 386 QFN---AYVLGQTSLSEVTGTQVAKANKEITDAQ 416
Cdd:cd13580   400 EENeniAVGPPTETLVSPTEKYGATLDKLEDDAF 433
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 51-344 8.89e-22

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 95.91  E-value: 8.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  51 QPIKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDvMLTQEADYV-RFAKNGVTMKLDDKLKDLgiDKSDFQPAV 129
Cdd:cd13657    18 QIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPD-LFIWAHDWIgQFAEAGLLVPISDYLSED--DFENYLPTA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 130 TDITNQVDGYYGFPQGFATEIMYYNKDMFDAAgvayPTddwTWDDYTAAAEKLTKADGSQYG----SDSPTFNGVWyslI 205
Cdd:cd13657    95 VEAVTYKGKVYGLPEAYETVALIYNKALVDQP----PE---TTDELLAIMKDHTDPAAGSYGlayqVSDAYFVSAW---I 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 206 GAAGDKVVDNGKLSFGNGLKKTLEFQKNLVDNKWQ--PQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATI 283
Cdd:cd13657   165 FGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPymPSDPSYNTQTSLFNEGKAAMIINGPWFIGGIKAAGIDLGVAPL 244

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937404779 284 PT---APGAKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMAD 344
Cdd:cd13657   245 PTvdgTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDD 308
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-325 1.70e-16

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 81.25  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWDDEMQPIKD------FIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPD-VMLTQEADYVRFAKNGVTMKLD 112
Cdd:cd13583     3 TLSMMYRDHPNYPVKDdwliwkEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDiIPVLYPGEENEFVASGALLPIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 113 DKLKDLG-----IDKSDFQPAVTDItNQVDG-YYGFPqGFATE-----IMYYNKDMFDAAGVAYPTddwTWDDYTAAAEK 181
Cdd:cd13583    83 DYLDYMPnykkyVEKWGLGKELATG-RQSDGkYYSLP-GLHEDpgvqySFLYRKDIFEKAGIKIPT---TWDEFYAALKK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 182 LTKADGSQY-------GSDSPTFNGVWYSL--IGAAGDKVVD--NGKLSFG---NGLKKTLEFQKNLV------------ 235
Cdd:cd13583   158 LKEKYPDSYpysdrwnSNALLLIAAPAFGTtaGWGFSNYTYDpdTDKFVYGattDEYKDMLQYFNKLYaeglldpesftq 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 236 -DNKWQPQPASGSKvsdMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIPTAPGAKKYNSLH-TSFWAINAKTKHSAAAE 313
Cdd:cd13583   238 tDDQAKAKFLNGKS---FVITTNPQTVDELQRNLRAADGGNYEVVSITPPAGPAGKAINGSRlENGFMISSKAKDSKNFE 314

                         330
                  ....*....|....*
gi 1937404779 314 KLVKF---LMSKEGQ 325
Cdd:cd13583   315 ALLQFldwLYSDEGQ 329
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 53-368 4.52e-14

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 72.28  E-value: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  53 IKDFIKANpDIKVKQIRVPGDDyntkLNQMIV---GGTAPDVMLTQEAD-YVRFAKNGVTMKLDDKLKDlGIDkSDFQPA 128
Cdd:COG1840     2 LEAFEKKT-GIKVNVVRGGSGE----LLARLKaegGNPPADVVWSGDADaLEQLANEGLLQPYKSPELD-AIP-AEFRDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 129 vtditnqvDGYYgFPQGFATEIMYYNKDMFDAAGVayPTddwTWDDYTAAAEKltkadgSQYGSDSPTFNGVWYSLIGAa 208
Cdd:COG1840    75 --------DGYW-FGFSVRARVIVYNTDLLKELGV--PK---SWEDLLDPEYK------GKIAMADPSSSGTGYLLVAA- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 209 gdkvvdngkLSFGNGLKKTLEFQKNLVDNKWQPQpASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIAtIPtapg 288
Cdd:COG1840   134 ---------LLQAFGEEKGWEWLKGLAANGARVT-GSSSAVAKAVASGEVAIGIVNSYYALRAKAKGAPVEVV-FP---- 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 289 aKKYNSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTPAFQSMMADGYYKVQGKNGPSNWSSLEASAKEA 368
Cdd:COG1840   199 -EDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGLPPLGELKLIDDDDKAAENREE 277
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 40-326 8.34e-12

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 64.94  E-value: 8.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTV--SYWDDEMQPIKD-FIKANPDIKVKQIRVPGDDYNTKLNQMIVGGT-APDVMLTQEA-DYVRFAKNGVTMKLDDK 114
Cdd:cd13547     1 KLVVytSMPEDLANALVEaFEKKYPGVKVEVFRAGTGKLMAKLAAEAEAGNpQADVLWVADPpTAEALKKEGLLLPYKSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 115 LKDlGIDKSDFQPavtditnqvDGYYgFPQGFATEIMYYNKDMFDAAGVayptddWTWDDYTAAAEKltkadgSQYGSDS 194
Cdd:cd13547    81 EAD-AIPAPFYDK---------DGYY-YGTRLSAMGIAYNTDKVPEEAP------KSWADLTKPKYK------GQIVMPD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 195 PTFNGVWYSLIGAAGDKvvdngklsFGNGLkktlEFQKNLVDNKWQPQPASGSkVSDMFAAGKAAMTLGGTwlVSTYKDV 274
Cdd:cd13547   138 PLYSGAALDLVAALADK--------YGLGW----EYFEKLKENGVKVEGGNGQ-VLDAVASGERPAGVGVD--YNALRAK 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937404779 275 DFKWDIATIPTAPGAkkynSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQK 326
Cdd:cd13547   203 EKGSPLEVIYPEEGT----VVIPSPIAILKGSKNPEAAKAFVDFLLSPEGQE 250
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
6-337 1.09e-11

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 65.70  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779   6 KRTVMRLVAGVAAVATLMGTAAcgssnssSSDDNTLTVSYWDDEMQP--IKDFIKANpDIKVKQirVPGDDYNTKLNQMI 83
Cdd:COG0687     3 RRSLLGLAAAALAAALAGGAPA-------AAAEGTLNVYNWGGYIDPdvLEPFEKET-GIKVVY--DTYDSNEEMLAKLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  84 VGGTAPDVMLTQEADYVRFAKNGVTMKLD-DKLKDLGIDKSDFQPAVTDITNQvdgyYGFPQGFATEIMYYNKDMFDAag 162
Cdd:COG0687    73 AGGSGYDVVVPSDYFVARLIKAGLLQPLDkSKLPNLANLDPRFKDPPFDPGNV----YGVPYTWGTTGIAYNTDKVKE-- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 163 vayPTDDWTW-------------DDYTAAAEKLTKADGSQYGSDSPTfngvwysLIGAAGDKvvdngklsfgngLKKtle 229
Cdd:COG0687   147 ---PPTSWADlwdpeykgkvallDDPREVLGAALLYLGYDPNSTDPA-------DLDAAFEL------------LIE--- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 230 fQKNLVDNKWqpqpASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIAtIPtAPGAkkynSLHTSFWAINAKTKHS 309
Cdd:COG0687   202 -LKPNVRAFW----SDGAEYIQLLASGEVDLAVGWSGDALALRAEGPPIAYV-IP-KEGA----LLWFDNMAIPKGAPNP 270

                         330       340
                  ....*....|....*....|....*...
gi 1937404779 310 AAAEKLVKFLMSKEGQKSMSQSLGNTPA 337
Cdd:COG0687   271 DLAYAFINFMLSPEVAAALAEYVGYAPP 298
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 40-336 7.66e-11

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 62.24  E-value: 7.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVSYWDDEMQP------IKDFIKANPdIKVKQIRVPGDDYntkLNQMIVGGTAP--DVMLTQEADYVRFAKNGVTMKL 111
Cdd:cd13589     1 TLVVATWGGSYEDaqrkavIEPFEKETG-IKVVYDTGTSADR---LAKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 112 D-DKLKDLGIDKsdfqPAVTDITNQVDGYYGFPQGFAteimyYNKDMFDAAgvayPTDDWTWDDytaaaekltkADGSQY 190
Cdd:cd13589    77 DySKIPNAAKDK----APAALKTGYGVGYTLYSTGIA-----YNTDKFKEP----PTSWWLADF----------WDVGKF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 191 GSDSPTFNGVWYSLIGAAGDKVVDNGKLSFGNGLKKTLEFQKNLVdnKWQPqpaSGSKVSDMFAAGKAAMTLGGTWLVST 270
Cdd:cd13589   134 PGPRILNTSGLALLEAALLADGVDPYPLDVDRAFAKLKELKPNVV--TWWT---SGAQLAQLLQSGEVDMAPAWNGRAQA 208

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937404779 271 YKDVDFKWDIatipTAPGAKKYNSLHTsfWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTP 336
Cdd:cd13589   209 LIDAGAPVAF----VWPKEGAILGPDT--LAIVKGAPNKELAMKFINFALSPEVQAALAEALGYGP 268
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 62-333 2.94e-08

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 55.40  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  62 DIKVKQIRVPGDDYNTKLNQMIVGGTAPDVML---TQEADYVRFAKNGVTMKLDD-------KLKDLGIDKSDFQPAVTD 131
Cdd:cd13581    31 GIKIEWETVPEDAWAEKKNLMLASGDLPDAFLgagASDADLMTYGKQGLFLPLEDlidkyapNLKALFDENPDIKAAITA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 132 ItnqvDGY-YGFP---QGFATEI---MYYNKDMFDAAGVAYPTddwTWDDY--------TAAAEKLTKAD-------GSQ 189
Cdd:cd13581   111 P----DGHiYALPsvnECYHCSYgqrMWINKKWLDKLGLEMPT---TTDELyevlkafkEQDPNGNGKADeiplsfsGLN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 190 YGSDSPTFngvwysLIGAAGDK---------VVDNGKL-SFGN--GLKKTLEF-----QKNLVDNKWQPQPASGSKvsdm 252
Cdd:cd13581   184 GGTDDPAF------LLNSFGINdggyggygfVVKDGKViYTATdpEYKEALAYlnklyKEGLIDPEAFTQDYDQLA---- 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 253 fAAGKAAMTLGG---TWLVSTYKDVDFKWDIATIP--TAP-GAKKYNSLHTSFW-----AINAKTKHSAAAEKLVKFLMS 321
Cdd:cd13581   254 -AKGKASTAKVGvffGWDPGLFFGEERYEQYVPLPplKGPnGDQLAWVGNSSGYgrggfVITSKNKNPEAAIRWADFLYS 332

                         330
                  ....*....|..
gi 1937404779 322 KEGqkSMSQSLG 333
Cdd:cd13581   333 PEG--SLQANFG 342
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 40-337 1.81e-07

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 52.73  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  40 TLTVsyW----DDEM--QPIKDFIKANPDIKVK-QIRVPG-DDYNTKLNQMIvgGTAPDVMLTQEADYVRFAKNGVTMKL 111
Cdd:cd13655     1 TLTV--WgpqeDQEWlkEMVDAFKEKHPEWKITiTIGVVGeADAKDEVLKDP--SAAADVFAFANDQLGELVDAGAIYPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 112 DDKLKDlgIDKSDFQPAVTDITNQVDGYYGFPQGFATEIMYYNKDMFDAAGVAyptddwTWDDYTAAAEKLTKadgsQYG 191
Cdd:cd13655    77 TGSAVD--KIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK------SLDTMLAKAPDAKG----KVS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 192 SDsptFNGVWY--SLIGAAGDKVV-----DNGKLSFGN--GLKKTlEFQKNLVDNKWQPQPASGSKVSdMFAAGKAAMTL 262
Cdd:cd13655   145 FD---LSNSWYlyAFFFGAGCKLFgnnggDTAGCDFNNekGVAVT-NYLVDLVANPKFVNDADGDAIS-GLKDGTLGAGV 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 263 GGTWLVSTYKDV---DFKwdIATIPTA-PGAKKY---NSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNT 335
Cdd:cd13655   220 SGPWDAANLKKAlgdNYA--VAKLPTYtLGGKDVqmkSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIG 297


                  ..
gi 1937404779 336 PA 337
Cdd:cd13655   298 PT 299
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 45-325 9.86e-07

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 50.92  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  45 YWDDEMQPIKDFIKANPDIKVKQIRVPGDDYNTKLNQMIVGGTAPDVMLTQ--EADYVRFAKNGVTMKLDDKLKDLGIDK 122
Cdd:cd13521    14 WVDDENWPVAKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADylKDKFIAYGMEGAFLPLSKYIDQYPNLK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 123 SDFQ--PAVTDITNQVDG-----YYGFPQGFATEIMYYNKDMFDAAGVAYPTddwTWDDYTAAAEKLTKADGSQYG-SDS 194
Cdd:cd13521    94 AFFKqhPDVLRASTASDGkiyliPYEPPKDVPNQGYFIRKDWLDKLNLKTPK---TLDELYNVLKAFKEKDPNGNGkADE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 195 PTFN-----GVWYSLIGAAGDKV----------VDNGKL-------SFGNGLKKTLEFQKN-LVDNKWQPQPASGSKvsD 251
Cdd:cd13521   171 IPFIdrdplYGAFRLINSWGARSaggstdsdwyEDNGKFkhpfaseEYKDGMKYMNKLYTEgLIDKESFTQKDDQAE--Q 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 252 MFAAGKAAMTLGGTWLVSTYKDVDFKWDIAT-----IPTAPGAKKYN------SLHTSFWAINAKTKHSAAAEKLVKFLM 320
Cdd:cd13521   249 KFSNGKLGGFTHNWFASDNLFTAQLGKEKPMyillpIAPAGNVKGRReedspgYTGPDGVAISKKAKNPVAALKFFDWLA 328


                  ....*
gi 1937404779 321 SKEGQ 325
Cdd:cd13521   329 SEEGR 333
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 73-324 9.50e-05

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 44.12  E-value: 9.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  73 DDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNGV--TMKLDDKLKDlgidksDFQPAVTDITNQVDGYYGFPQGFATEI 150
Cdd:cd13656    37 DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLlaEITPDKAFQD------KLYPFTWDAVRYNGKLIAYPIAVEALS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 151 MYYNKDMFdaagvayPTDDWTWDDYTAAAEKLTKADGSQ--YGSDSPTFNgvwYSLIGAAGDKVV--DNGKLSFGN---- 222
Cdd:cd13656   111 LIYNKDLL-------PNPPKTWEEIPALDKELKAKGKSAlmFNLQEPYFT---WPLIAADGGYAFkyENGKYDIKDvgvd 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 223 --GLKKTLEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIPTAPGAKKYNSLHTSFW 300
Cdd:cd13656   181 naGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSA 260

                         250       260
                  ....*....|....*....|....*
gi 1937404779 301 AINAKTKHSA-AAEKLVKFLMSKEG 324
Cdd:cd13656   261 GINAASPNKElAKEFLENYLLTDEG 285
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 136-336 2.54e-04

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 42.29  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 136 VDGYY----GFPQGFAteimyYNKDMFDAAGVAyptddWTWDDYTAAAEKltkadgSQYGSDSPTFNGVWYSLIGAA--- 208
Cdd:cd13518    89 PDGYWvgfaARARVFI-----YNTDKLKEPDLP-----KSWDDLLDPKWK------GKIVYPTPLRSGTGLTHVAALlql 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 209 -GDkvvDNGKLSFGNGLKKTLEFqknlvdnkwqpqPASGSKVSDMFAAGKAAMTLGGTWLVstYKDVDFKWDIATIPTAP 287
Cdd:cd13518   153 mGE---EKGGWYLLKLLANNGKP------------VAGNSDAYDLVAKGEVAVGLTDTYYA--ARAAAKGEPVEIVYPDQ 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1937404779 288 GAkkynSLHTSFWAINAKTKHSAAAEKLVKFLMSKEGQKSMSQSLGNTP 336
Cdd:cd13518   216 GA----LVIPEGVALLKGAPNPEAAKKFIDFLLSPEGQKALAAANAQLP 260
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
63-288 6.10e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 41.92  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  63 IKVKqIRVPgDDYNTKLNQMIVGGTAPDVMLTQEADYVRFAKNG------VTMKLDDKLKDLGIDksdfqpAVTditnqV 136
Cdd:PRK09474   59 IKVT-VEHP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGllaevtPSKAFKDKLVPFTWD------AVR-----Y 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 137 DG-YYGFPQGFATEIMYYNKDMFdaagvayPTDDWTWDDYTAAAEKLtKADGSQ---YGSDSPTFNgvwYSLIGAAGDKV 212
Cdd:PRK09474  126 NGkLIGYPIAVEALSLIYNKDLV-------PTPPKTWEEIPALDKEL-KAKGKSaimWNLQEPYFT---WPLIAADGGYA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 213 --VDNGKLSFGN------GLKKTLEFQKNLVDNKWQPQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIATIP 284
Cdd:PRK09474  195 fkFENGGYDVKDvgvnnaGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINYGVTVLP 274


                  ....
gi 1937404779 285 TAPG 288
Cdd:PRK09474  275 TFNG 278
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
55-185 6.99e-04

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 41.71  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  55 DFIKANPDIKVkqIRVPGDDYNTKLNQMIVG---GTAPDVMLTQEADYVRFAKNGVTMKLDDKLKDLGI--DKSDFQPAV 129
Cdd:PRK10974   48 RFNASQPDYKI--VPVYKGNYEQSLAAGIAAfrsGNAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIpfDESQFVPTV 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937404779 130 TditnqvdGYY---------GFPQGFATEIMYYNKDMFDAAGVAYPTDDWTWDDYTAAAEKLTKA 185
Cdd:PRK10974  126 A-------GYYsdaktghllSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAA 183
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 89-337 2.14e-03

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 39.65  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  89 PDVMLTQEADYV------RFAKNGVtmklddkLKDLGIDKSDFQPAVTDITNQVD--GYYGfPQGFATEIMYYNKDMFDa 160
Cdd:pfam13343   4 PDIILSAGDLFFdkrfleKFIEEGL-------FQPLDSANLPNVPKDFDDEGLRDpdGYYT-PYGVGPLVIAYNKERLG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 161 aGVAYPTddwTWDDYTaaaekltkadgsqygsdSPTFNGvwysLIGAAGDKVVDNGK-----LSFGNGLKKTLEFQKNLV 235
Cdd:pfam13343  75 -GRPVPR---SWADLL-----------------DPEYKG----KVALPGPNVGDLFNalllaLYKDFGEDGVRKLARNLK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 236 DNKwqpQPASGSKVSDMFAAGKAAMTLGGTWLVSTYKDVDFKWDIAtIPtAPGAkkynSLHTSFWAInaKTKHSAAAEKL 315
Cdd:pfam13343 130 ANL---HPAQMVKAAGRLESGEPAVYLMPYFFADILPRKKKNVEVV-WP-EDGA----LVSPIFMLV--KKGKKELADPL 198

                         250       260
                  ....*....|....*....|..
gi 1937404779 316 VKFLMSKEGQKSMSQSLGNTPA 337
Cdd:pfam13343 199 IDFLLSPEVQAILAKAGLVFPV 220
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 78-324 5.49e-03

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 38.96  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779  78 KLNQMIVGGTAPDVMLTQEADYV----RFAKNGVTMKLDD-------KLKDLGIDKSDFQPAVTDITNQVDGYYGFPQGF 146
Cdd:cd13584    48 QFNLMMASGQLPDIIGGDWLKDKggfeKYGEDGAFLPLNDlidqyapNLKKFLDEHPDVKKAITTDDGNIYGFPYLPDGD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 147 ATEIMY---YNKDMFDAAGVAYPT--DDWtWDDYTAAAEKltKADGSQYGSDSPTFNGVW-----YSLIGAAG---DKVV 213
Cdd:cd13584   128 VAKEARgyfIRKDWLDKLGLKTPStiDEW-YTVLKAFKER--DPNGNGKADEVPLILTKPgydetGRLINAWGaymDFYQ 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937404779 214 DNGKLSFG-------NGLKKTLEFQKN-LVD-------NKWQPQ----PASGSKVSDMFAAGKAAMTLggtwlvSTYKDV 274
Cdd:cd13584   205 ENGKVKYGplepgfkDFLKTMNQWYKEgLIDpdfftrkAKAREQnimnGNIGGFTHDWFASTGTFNLA------LLKNVP 278

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937404779 275 DFKWDIATIPTAPGAKKYNSLHTSF------WAINAKTKHSAAAEKLVKFLMSKEG 324
Cdd:cd13584   279 DFKLVAVPPPVLNKGQTPYEEDSRQiakgdgAAITASNKNPVLAIKWLDYAYSEEG 334
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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