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Conserved domains on  [gi|2265658632|ref|WP_253418337|]
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ABC transporter substrate-binding protein [Pantoea sp. B550]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10100138)

ABC transporter substrate-binding protein functions as the initial receptor in the active ABC transport of one or more from a variety of substrates such as metal ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 11-350 7.82e-145

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


:

Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 413.24  E-value: 7.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  11 TLTDITGRQVTIPDHPQRIMLGESRMLYSVALLMPGNPLQHIAGWPQDLKKYDPQTWQVFARQFPQMETIPVVGLDGVND 90
Cdd:cd01139     2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  91 VNPEQVVALKPDVVILPQLARDSENVAVLEKMLAAAHIPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQFNHFYRSH 170
Cdd:cd01139    82 FSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 171 MQRISSRLADYHGPKPSVLLQLHLGRRSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYYFATG 250
Cdd:cd01139   162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIATG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 251 TGSADEAGALKLGPAVTTAQTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYLSPWHVVATEFFAATLYPQLFRDVDP 330
Cdd:cd01139   242 GNWAKDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDLDP 321

                         330       340
                  ....*....|....*....|
gi 2265658632 331 EQTLQQLFRDFLPIPFSGSY 350
Cdd:cd01139   322 EATLQEFHRQFLPVDYSGTF 341
 
Name Accession Description Interval E-value
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 11-350 7.82e-145

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 413.24  E-value: 7.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  11 TLTDITGRQVTIPDHPQRIMLGESRMLYSVALLMPGNPLQHIAGWPQDLKKYDPQTWQVFARQFPQMETIPVVGLDGVND 90
Cdd:cd01139     2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  91 VNPEQVVALKPDVVILPQLARDSENVAVLEKMLAAAHIPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQFNHFYRSH 170
Cdd:cd01139    82 FSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 171 MQRISSRLADYHGPKPSVLLQLHLGRRSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYYFATG 250
Cdd:cd01139   162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIATG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 251 TGSADEAGALKLGPAVTTAQTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYLSPWHVVATEFFAATLYPQLFRDVDP 330
Cdd:cd01139   242 GNWAKDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDLDP 321

                         330       340
                  ....*....|....*....|
gi 2265658632 331 EQTLQQLFRDFLPIPFSGSY 350
Cdd:cd01139   322 EATLQEFHRQFLPVDYSGTF 341
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 11-356 2.93e-67

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 216.69  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  11 TLTDITGRQVTIPDHPQRIMLGESRMLYSVALLMPgNPLQHIAGWPQDLKKYDPQTWQVFARQFPQMETIPVVGLDGVND 90
Cdd:PRK14048   33 TVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHP-DPVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDGSGPG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  91 VNPEQVVALKPDVVILPQLARDSEN----VAVLEKMlaaaHIPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQFNHF 166
Cdd:PRK14048  112 LSFETILTLKADLAILANWQADTEAgqraIEYLESI----GVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 167 YRSHMQRISSRLADYHGPKPSVLLQLHLGRrSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYY 246
Cdd:PRK14048  188 YEERLARIRDRVAKHSEPGPTVLMEAFPAA-DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVY 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 247 FATGTGSADEAGaLKLGPAVTtAQTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYLSPWHVVATEFFAATLYPQLFR 326
Cdd:PRK14048  267 IATSSPGGKYSG-FSIGPGVS-AEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRPELFA 344

                         330       340       350
                  ....*....|....*....|....*....|
gi 2265658632 327 DVDPEQTLQQLFRDFLPIPFSGSYLYRLAP 356
Cdd:PRK14048  345 DIDPAATLAEINRRFAAVPFEGSYWISLKK 374
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 28-326 5.59e-44

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 152.84  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  28 RIMLGESRMLYSVALLmpgNPLQHIAGWPQDLKKYDPQTwqvfarqfpQMETIPVVGldGVNDVNPEQVVALKPDVVILP 107
Cdd:COG0614     2 RIVSLSPSATELLLAL---GAGDRLVGVSDWGYCDYPEL---------ELKDLPVVG--GTGEPNLEAILALKPDLVLAS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 108 QLARDSENVAVLEKmlaaAHIPVVKIDLRvnLLKNTERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADyHGPKPS 187
Cdd:COG0614    68 SSGNDEEDYEQLEK----IGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG-AEERPT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 188 VLLQLHLGrrSECCVTSVNGNLGELLTFAGGNNIASqQIKGVFGRLSEESVIAAQPDYYFATGTGSADEagalklgpavt 267
Cdd:COG0614   141 VLYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAA-DLGGGYPEVSLEQVLALDPDVIILSGGGYDAE----------- 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265658632 268 taqTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYL--SPWHVVATEFFAATLYPQLFR 326
Cdd:COG0614   207 ---TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLLSrpGPRLLLALEDLAKALHPELFA 264
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 75-253 1.39e-14

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 72.40  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  75 PQMETIPVVGLDGvnDVNPEQVVALKPDVVILPQLARDSEnvavlEKMLAAAHIPVVKIDLRVNLLKNTERsITLLGEVL 154
Cdd:pfam01497  34 DAVAAIVKVGAYG--EINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIFESSSTGESLKEQ-IKQLGELL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 155 NQPQRAAQFNHFYRSHMQRISSRlADYHGPKPSVLLQLHLGRrseccVTSVNGN---LGELLTFAGGNNIASQQIKGVFG 231
Cdd:pfam01497 106 GLEDEAEELVAEIDSALAAAKKA-VPSLTRKPVLVFGGADGG-----GYVVAGSntyIGDLLRILGIENIAAELSGSEYA 179

                         170       180
                  ....*....|....*....|..
gi 2265658632 232 RLSEESVIAAQPDYYFATGTGS 253
Cdd:pfam01497 180 PISFEAILSSNPDVIIVSGRDS 201
 
Name Accession Description Interval E-value
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 11-350 7.82e-145

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 413.24  E-value: 7.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  11 TLTDITGRQVTIPDHPQRIMLGESRMLYSVALLMPGNPLQHIAGWPQDLKKYDPQTWQVFARQFPQMETIPVVGLDGVND 90
Cdd:cd01139     2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  91 VNPEQVVALKPDVVILPQLARDSENVAVLEKMLAAAHIPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQFNHFYRSH 170
Cdd:cd01139    82 FSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 171 MQRISSRLADYHGPKPSVLLQLHLGRRSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYYFATG 250
Cdd:cd01139   162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIATG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 251 TGSADEAGALKLGPAVTTAQTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYLSPWHVVATEFFAATLYPQLFRDVDP 330
Cdd:cd01139   242 GNWAKDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDLDP 321

                         330       340
                  ....*....|....*....|
gi 2265658632 331 EQTLQQLFRDFLPIPFSGSY 350
Cdd:cd01139   322 EATLQEFHRQFLPVDYSGTF 341
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 11-356 2.93e-67

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 216.69  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  11 TLTDITGRQVTIPDHPQRIMLGESRMLYSVALLMPgNPLQHIAGWPQDLKKYDPQTWQVFARQFPQMETIPVVGLDGVND 90
Cdd:PRK14048   33 TVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHP-DPVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDGSGPG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  91 VNPEQVVALKPDVVILPQLARDSEN----VAVLEKMlaaaHIPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQFNHF 166
Cdd:PRK14048  112 LSFETILTLKADLAILANWQADTEAgqraIEYLESI----GVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 167 YRSHMQRISSRLADYHGPKPSVLLQLHLGRrSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYY 246
Cdd:PRK14048  188 YEERLARIRDRVAKHSEPGPTVLMEAFPAA-DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVY 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 247 FATGTGSADEAGaLKLGPAVTtAQTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYLSPWHVVATEFFAATLYPQLFR 326
Cdd:PRK14048  267 IATSSPGGKYSG-FSIGPGVS-AEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRPELFA 344

                         330       340       350
                  ....*....|....*....|....*....|
gi 2265658632 327 DVDPEQTLQQLFRDFLPIPFSGSYLYRLAP 356
Cdd:PRK14048  345 DIDPAATLAEINRRFAAVPFEGSYWISLKK 374
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 28-326 5.59e-44

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 152.84  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  28 RIMLGESRMLYSVALLmpgNPLQHIAGWPQDLKKYDPQTwqvfarqfpQMETIPVVGldGVNDVNPEQVVALKPDVVILP 107
Cdd:COG0614     2 RIVSLSPSATELLLAL---GAGDRLVGVSDWGYCDYPEL---------ELKDLPVVG--GTGEPNLEAILALKPDLVLAS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 108 QLARDSENVAVLEKmlaaAHIPVVKIDLRvnLLKNTERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADyHGPKPS 187
Cdd:COG0614    68 SSGNDEEDYEQLEK----IGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG-AEERPT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 188 VLLQLHLGrrSECCVTSVNGNLGELLTFAGGNNIASqQIKGVFGRLSEESVIAAQPDYYFATGTGSADEagalklgpavt 267
Cdd:COG0614   141 VLYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAA-DLGGGYPEVSLEQVLALDPDVIILSGGGYDAE----------- 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265658632 268 taqTRQSLLALTSQQNALKQLTALRDGHAGAIWHNFYL--SPWHVVATEFFAATLYPQLFR 326
Cdd:COG0614   207 ---TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLLSrpGPRLLLALEDLAKALHPELFA 264
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 4-330 4.19e-35

Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 130.17  E-value: 4.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632   4 SACAHSRTLTDITGRQVTIPDHPQRImlgesrmlysVALLMPGNPLQHIAGwPQDLKKYDPQTWQ---VFARQFPQMETI 80
Cdd:cd01142     2 AATAATRTITDMAGRKVTIPDEVKRI----------AALWGAGNAVVAALG-GGKLIVATTSTVQqepWLYRLAPSLENV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  81 PVVGLDgvNDVNPEQVVALKPDVVILPQLARDSENVAVLEKmlaaahipvvkidLRVNLLKNTE-----RSITLLGEVLN 155
Cdd:cd01142    71 ATGGTG--NDVNIEELLALKPDVVIVWSTDGKEAGKAVLRL-------------LNALSLRDAEleevkLTIALLGELLG 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 156 QPQRAAQFNHFYRSHMQRISSRLADY-HGPKPSVllqLHLGRRseccVTSVNGN---LGELLTFAGGNNIASQQIKGVFG 231
Cdd:cd01142   136 RQEKAEALVAYFDDNLAYVAARTKKLpDSERPRV---YYAGPD----PLTTDGTgsiTNSWIDLAGGINVASEATKKGSG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 232 RLSEESVIAAQPDYYFatgTGSADEAGALKLGPavttaqtrqsllaltsqqnALKQLTALRDghaGAIWHN-FYLSPWHV 310
Cdd:cd01142   209 EVSLEQLLKWNPDVII---VGNADTKAAILADP-------------------RWQNLRAVKN---GRVYVNpEGAFWWDR 263

                         330       340
                  ....*....|....*....|....*.
gi 2265658632 311 VATE------FFAATLYPQLFRDVDP 330
Cdd:cd01142   264 PSAEeallglWLAKTLYPERFTDDDM 289
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 52-282 2.22e-18

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 83.54  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  52 IAGWpqDLKKYDPQTwQVFARQFPQMETIPVVG-LDGVNDVNPEQVVALKPDVVILPQLARDSENVAVLEKMLAaahIPV 130
Cdd:cd01147    28 IVGV--DDAEKSDEG-RPYFLASPELKDLPVIGrGGRGNTPNYEKIAALKPDVVIDVGSDDPTSIADDLQKKTG---IPV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 131 VKIDLRvNLLKNTERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADYH-GPKPSVllqlHLGRRSEC----CVTSV 205
Cdd:cd01147   102 VVLDGG-DSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPdEEKPTV----YFGRIGTKgaagLESGL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265658632 206 NGNlGELLTFAGGNNIASQQIKGVFGRLSEESVIAAQPDYYFATgtgsaDEAGALKLGPAVTTAQTRQSLLALTSQQ 282
Cdd:cd01147   177 AGS-IEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLD-----TGSFYLSLEGYAKNRPFWQSLKAVKNGR 247
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 68-272 1.30e-15

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 76.00  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  68 QVFAR----QFP-QMETIPVVGldGVNDVNPEQVVALKPDVVILPQLARDSENVAVLEkmlaAAHIPVVKIDLRVNLlKN 142
Cdd:COG4558    49 RLVGVdttsTYPaAAKALPDVG--YMRQLSAEGILSLKPTLVLASEGAGPPEVLDQLR----AAGVPVVVVPAAPSL-EG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 143 TERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADyHGPKPSVLLQLHLGRRSeccvTSVNGN---LGELLTFAGGN 219
Cdd:COG4558   122 VLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAA-IGKPPRVLFLLSRGGGR----PMVAGRgtaADALIRLAGGV 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2265658632 220 NIAsQQIKGvFGRLSEESVIAAQPDYYFATGTG---SADEAGALKLgPAVttAQTR 272
Cdd:COG4558   197 NAA-AGFEG-YKPLSAEALIAAAPDVILVMTRGlesLGGVDGLLAL-PGL--AQTP 247
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 73-189 1.77e-15

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 72.98  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  73 QFPQMETIPVVGldGVNDVNPEQVVALKPDVVIlpqlARDSENVAVLEKmLAAAHIPVVKIDLRVNL-LKNTERSITLLG 151
Cdd:cd00636    36 AKALLEKVPDVG--HGYEPNLEKIAALKPDLII----ANGSGLEAWLDK-LSKIAIPVVVVDEASELsLENIKESIRLIG 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2265658632 152 EVLNQPQRAAQFNHFYRSHMQRISSRLADYHGPKPSVL 189
Cdd:cd00636   109 KALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 75-244 4.78e-15

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 72.70  E-value: 4.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  75 PQMETIPVVGldGVNDVNPEQVVALKPDVVILpqlarDSENVAVLEKMLAAAHIPVVKIDLRVNlLKNTERSITLLGEVL 154
Cdd:cd01143    37 KEVRKKPKVG--SYSNPNVEKIVALKPDLVIV-----SSSSLAELLEKLKDAGIPVVVLPAASS-LDEIYDQIELIGKIT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 155 NQPQRAAQFNHfyrsHMQRISSRLAD--YHGPKPSVLLQLHLGRrseccVTSVNGN--LGELLTFAGGNNIASqQIKGvF 230
Cdd:cd01143   109 GAEEEAEKLVK----EMKQKIDKVKDkgKTIKKSKVYIEVSLGG-----PYTAGKNtfINELIRLAGAKNIAA-DSGG-W 177

                         170
                  ....*....|....
gi 2265658632 231 GRLSEESVIAAQPD 244
Cdd:cd01143   178 PQVSPEEILKANPD 191
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 75-252 1.09e-14

Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238564 [Multi-domain]  Cd Length: 245  Bit Score: 72.72  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  75 PQMETIPVVGLDGvnDVNPEQVVALKPDVVIlpqlARDSENVAVLEKMLAAAHIPVVkiDLRVNLLKNTERSITLLGEVL 154
Cdd:cd01144    34 PEAKKLPRVGGFY--QLDLERVLALKPDLVI----AWDDCNVCAVVDQLRAAGIPVL--VSEPQTLDDILADIRRLGTLA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 155 NQPQRAAQFNHFYRSHMQRISSRLADYhgPKPSVLLQLHlgrrSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFgRLS 234
Cdd:cd01144   106 GRPARAEELAEALRRRLAALRKQYASK--PPPRVFYQEW----IDPLMTAGGDWVPELIALAGGVNVFADAGERSP-QVS 178

                         170
                  ....*....|....*...
gi 2265658632 235 EESVIAAQPDYYFATGTG 252
Cdd:cd01144   179 WEDVLAANPDVIVLSPCG 196
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 75-253 1.39e-14

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 72.40  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  75 PQMETIPVVGLDGvnDVNPEQVVALKPDVVILPQLARDSEnvavlEKMLAAAHIPVVKIDLRVNLLKNTERsITLLGEVL 154
Cdd:pfam01497  34 DAVAAIVKVGAYG--EINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIFESSSTGESLKEQ-IKQLGELL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 155 NQPQRAAQFNHFYRSHMQRISSRlADYHGPKPSVLLQLHLGRrseccVTSVNGN---LGELLTFAGGNNIASQQIKGVFG 231
Cdd:pfam01497 106 GLEDEAEELVAEIDSALAAAKKA-VPSLTRKPVLVFGGADGG-----GYVVAGSntyIGDLLRILGIENIAAELSGSEYA 179

                         170       180
                  ....*....|....*....|..
gi 2265658632 232 RLSEESVIAAQPDYYFATGTGS 253
Cdd:pfam01497 180 PISFEAILSSNPDVIIVSGRDS 201
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 73-278 1.58e-12

Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238569 [Multi-domain]  Cd Length: 235  Bit Score: 66.52  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  73 QFPQMET-IPVVGLdgVNDVNPEQVVALKPDVVILPQLARDSENVAVLEkmlaAAHIPVVKIDlRVNLLKNTERSITLLG 151
Cdd:cd01149    32 TYPEAAAkLPDVGY--MRQLSAEGVLSLKPTLVIASDEAGPPEALDQLR----AAGVPVVTVP-STPTLDGLLTKIRQVA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 152 EVLNQPQRAAQFNHFYRSHMQRISSRLADYHGPKPSVLLQLHLGRRSEccVTSVNGNLGELLTFAGGNNIAsQQIKGvFG 231
Cdd:cd01149   105 QALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAM--AAGRNTAADAIIALAGAVNAA-AGFRG-YK 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2265658632 232 RLSEESVIAAQPDYYFAT---GTGSADEAGALKL-GPAVTTAQTRQSLLAL 278
Cdd:cd01149   181 PLSAEALIAAQPDVILVMsrgLDAVGGVDGLLKLpGLAQTPAGRNKRILAM 231
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 5-249 9.89e-09

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 56.46  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632   5 ACAHSRTLTDITGRQVTIPDHPQRIMLgesrmlysvallmpgnplqhiagwpqdLKKYDPQT-WQVFARQfpqmetiPVV 83
Cdd:PRK09534   39 ACSFPVTETDATGTEITLDERPERVVT---------------------------LNPSAAQTmWELGARD-------RVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  84 G-------LDGVND-----------VNPEQVVALKPDVVILPQLARDSENVAVLEKMLAAAHIPVVkidlrvNLLKNTER 145
Cdd:PRK09534   85 GvtqyasyLDGAEErtnvsggqpfgVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAA------TSIEDVAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 146 SITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADYHGpKPSVLLQLHLGRrseccVTSVNGNLGELLTFAGGNNIASQQ 225
Cdd:PRK09534  159 KTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDD-RPRVLYPLGDGY-----TAGGNTFIGALIEAAGGHNVAADA 232

                         250       260
                  ....*....|....*....|....
gi 2265658632 226 IKGVFGRLSEESVIAAQPDYYFAT 249
Cdd:PRK09534  233 TTDGYPQLSEEVIVQQDPDVIVVA 256
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 19-258 2.98e-05

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 44.94  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  19 QVTIPDHPQRIMLGESRMLYSVALL------MPGNPLQhiagwPQDLKKYdpqtwqvfarqfpQMETIPVVGldGVNDVN 92
Cdd:cd01140     5 ETKVPKNPEKVVVFDVGALDTLDALgvkvvgVPKSSTL-----PEYLKKY-------------KDDKYANVG--TLFEPD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  93 PEQVVALKPDVVILPQLARDSenvavLEKMLAAAHIPVVKIDLRvNLLKNTERSITLLGEVLNQPQRAAQFNhfyrshmQ 172
Cdd:cd01140    65 LEAIAALKPDLIIIGGRLAEK-----YDELKKIAPTIDLGADLK-NYLESVKQNIETLGKIFGKEEEAKELV-------A 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 173 RISSRLA---DYHGPKPSVLLQLHLGRRseccvTSVNGN---LGELLTFAGGNNIASQQIKGVFGR-LSEESVIAAQPDY 245
Cdd:cd01140   132 EIDASIAeakSAAKGKKKALVVLVNGGK-----LSAFGPgsrFGWLHDLLGFEPADENIKASSHGQpVSFEYILEANPDW 206

                         250
                  ....*....|...
gi 2265658632 246 YFATGTGSADEAG 258
Cdd:cd01140   207 LFVIDRGAAIGAE 219
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 76-267 3.66e-05

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 45.02  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  76 QMETIPVVGldgvnDVNP--EQVVALKPDVVIlpqlARDS----ENVAVLEKMLAAAHIPV-------VKIDLRVNlLKN 142
Cdd:cd01148    58 KYDKVPELA-----KKYPskETVLAARPDLVF----GGWSygfdKGGLGTPDSLAELGIKTyilpescGQRRGEAT-LDD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 143 TERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADyHGPKPSVLLQLHLGRRSeccVTSVNGNL-GELLTFAGGNNI 221
Cdd:cd01148   128 VYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKG-DGKKVAVFVYDSGEDKP---FTSGRGGIpNAIITAAGGRNV 203

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265658632 222 AsQQIKGVFGRLSEESVIAAQPDYY----FATGTGSADEAGALKLGPAVT 267
Cdd:cd01148   204 F-ADVDESWTTVSWETVIARNPDVIviidYGDQNAAEQKIKFLKENPALK 252
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 58-264 6.73e-05

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 43.81  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  58 DLKKYDPqtWQVFARQfpQMETIPVVGLDGvnDVNPEQVVALKPDVVILPQlARDSENVAVLEKmLAaahiPVVKIDLRv 137
Cdd:cd01146    29 DTAGYKP--WIPEPAL--PLEGVVDVGTRG--QPNLEAIAALKPDLILGSA-SRHDEIYDQLSQ-IA----PTVLLDSS- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 138 NLLKNTERSITLLGEVLNQPQRAAQFNHFYRSHMQRISSRLADYHGPKPSVllqLHLGRRSECCVTSVNGNLGELLTFAG 217
Cdd:cd01146    96 PWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSV---VRFSDAGSIRLYGPNSFAGSVLEDLG 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2265658632 218 GNNIASQQI--KGVFGRLSEESVIAAQPDYYFATGTGSADEAGALKLGP 264
Cdd:cd01146   173 LQNPWAQETtnDSGFATISLERLAKADADVLFVFTYEDEELAQALQANP 221
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 20-260 1.85e-04

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 42.32  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  20 VTIPDHPQRI-MLGESRMLYsvaLLMPGNPLQHIAgWPQDLKKYdpqtwqvfarqfpqMETIPVVGLDGVNDVNPEQVVA 98
Cdd:cd01138     3 VEIPAKPKRIvALSGETEGL---ALLGIKPVGAAS-IGGKNPYY--------------KKKTLAKVVGIVDEPNLEKVLE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  99 LKPDVVILpqLARDSENVAVLEKMLAAAHIPVVKIDLRVNLLkntersitLLGEVLNQPQRAAQFNHFYRSHMQRISSRL 178
Cdd:cd01138    65 LKPDLIIV--SSKQEENYEKLSKIAPTVPVSYNSSDWEEQLK--------EIGKLLNKEDEAEKWLADYKQKAKEAKEKI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 179 ADYHGPKPSVLLqlhLGRRSECCVTSVNGNLGELLTFAGGNNIASQQIKGVFGR-----LSEESVIAAQPDYYFATGTgS 253
Cdd:cd01138   135 KKKLGNDKSVAV---LRGRKQIYVFGEDGRGGGPILYADLGLKAPEKVKEIEDKpgyaaISLEVLPEFDADYIFLLFF-T 210


                  ....*..
gi 2265658632 254 ADEAGAL 260
Cdd:cd01138   211 GPEAKAD 217
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 7-324 1.44e-03

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 39.90  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632   7 AHSRTLTDITGrQVTIPDHPQRIMLGESRMLYSVALL--MP-GnplqhIAgwpqDLKKYDPqtWQVFARqfPQMETIPVV 83
Cdd:COG4594    34 AGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALgvTPvG-----IA----DDNDYDR--WVPYLR--DLIKGVTSV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632  84 GLDgvNDVNPEQVVALKPDVVIlpqlARDSENVAVLEKMLAAAhiPVVKIDLRVNLLKNTERSITLLGEVLNQPQRAAQF 163
Cdd:COG4594   100 GTR--SQPNLEAIAALKPDLII----ADKSRHEAIYDQLSKIA--PTVLFKSRNGDYQENLESFKTIAKALGKEEEAEAV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 164 NHFYRSHMQRISSRLADYHGPKPSVLLQ-------LHLGrrseccvtsvNGNLGELLTFAGGNNIASQQIKGVFG--RLS 234
Cdd:COG4594   172 LADHDQRIAEAKAKLAAADKGKKVAVGQfradglrLYTP----------NSFAGSVLAALGFENPPKQSKDNGYGysEVS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265658632 235 EESVIAAQPD--YYFATGTGSADEAGalklgpavttaqtrqsllaltsQQNAL-KQLTALRDGHA----GAIWhNFYLSP 307
Cdd:COG4594   242 LEQLPALDPDvlFIATYDDPSILKEW----------------------KNNPLwKNLKAVKNGRVyevdGDLW-TRGRGP 298

                         330
                  ....*....|....*..
gi 2265658632 308 whvVATEFFAATLYPQL 324
Cdd:COG4594   299 ---LAAELMADDLVEIL 312
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 90-160 1.78e-03

Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238561 [Multi-domain]  Cd Length: 186  Bit Score: 38.94  E-value: 1.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265658632  90 DVNPEQVVALKPDVVILPQLardSENVAVLEKmLAAAHIPVVKIDLRVNLLKNTErSITLLGEVLNQPQRA 160
Cdd:cd01141    59 SLNVELIVALKPDLVILYGG---FQAQTILDK-LEQLGIPVLYVNEYPSPLGRAE-WIKFAAAFYGVGKED 124
 
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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