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Conserved domains on  [gi|81913588|sp|Q8BSY0|]
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RecName: Full=Aspartyl/asparaginyl beta-hydroxylase; AltName: Full=Aspartate beta-hydroxylase; Short=ASP beta-hydroxylase; AltName: Full=Peptide-aspartate beta-dioxygenase

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 574-728 2.34e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 2.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   574 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 650
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588   651 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 728
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 52-117 8.55e-39

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 137.67  E-value: 8.55e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81913588    52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 316-531 2.04e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.94  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 316 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 394
Cdd:COG2956  34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 395 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 474
Cdd:COG2956 107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588 475 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG2956 182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 574-728 2.34e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 2.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   574 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 650
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588   651 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 728
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 570-735 2.88e-54

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 186.24  E-value: 2.88e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 570 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCALLEKFsettgcr 644
Cdd:COG3555  20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 645 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 720
Cdd:COG3555  93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                       170
                ....*....|....*
gi 81913588 721 FIVDVWHPELTPQQR 735
Cdd:COG3555 172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 52-117 8.55e-39

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 137.67  E-value: 8.55e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81913588    52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 316-531 2.04e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.94  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 316 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 394
Cdd:COG2956  34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 395 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 474
Cdd:COG2956 107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588 475 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG2956 182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 324-510 2.28e-07

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 54.32  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   324 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAADL-PDAPTD-- 400
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   401 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLLGDN 453
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81913588   454 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTDDGRF 510
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 328-398 9.78e-06

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 43.86  E-value: 9.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81913588   328 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL-PDAP 398
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 574-728 2.34e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 2.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   574 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 650
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588   651 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 728
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 570-735 2.88e-54

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 186.24  E-value: 2.88e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 570 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCALLEKFsettgcr 644
Cdd:COG3555  20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 645 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 720
Cdd:COG3555  93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                       170
                ....*....|....*
gi 81913588 721 FIVDVWHPELTPQQR 735
Cdd:COG3555 172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 52-117 8.55e-39

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 137.67  E-value: 8.55e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81913588    52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 316-531 2.04e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.94  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 316 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 394
Cdd:COG2956  34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 395 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 474
Cdd:COG2956 107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81913588 475 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG2956 182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
334-499 2.51e-13

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 2.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 334 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADL-PDAPTdlvklSLKRRSER 412
Cdd:COG0457  18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 413 QQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIP 492
Cdd:COG0457  86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                ....*..
gi 81913588 493 YLKEGIE 499
Cdd:COG0457 166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 326-499 6.42e-11

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 60.59  E-value: 6.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 326 AELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddlaekqrsnevlrraietYQEAADLPDAptdlvkls 405
Cdd:COG4783   6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI--------------------LLQLGDLDEA-------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 406 lkrrserqqflghmrgsLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQN 485
Cdd:COG4783  58 -----------------IVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                       170
                ....*....|....
gi 81913588 486 KISESIPYLKEGIE 499
Cdd:COG4783 121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 324-513 4.73e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.09  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 324 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYgkaqcedDLAEKQRSNEVLRRAIETYQEAADL-PDAPTDLV 402
Cdd:COG3914  78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 403 KLSLKRRSerqqfLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILK 482
Cdd:COG3914 151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                       170       180       190
                ....*....|....*....|....*....|.
gi 81913588 483 AQNKISESIPYLKEGIESGDPGTDDGRFYFH 513
Cdd:COG3914 226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
416-531 7.13e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.02  E-value: 7.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 416 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLK 495
Cdd:COG0457  21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 81913588 496 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG0457 101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
355-549 1.07e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.64  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 355 PQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADlpdaptdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFP 434
Cdd:COG0457   5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAE-----------ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 435 SDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHL 514
Cdd:COG0457  74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 81913588 515 GDAMQRVGN-KEAYKWYELGHKRGHFASVWQRSLYN 549
Cdd:COG0457 151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 350-500 5.00e-09

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 55.74  E-value: 5.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 350 LVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRL 429
Cdd:COG5010   1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81913588 430 VQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIES 500
Cdd:COG5010  81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 333-435 2.09e-08

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 52.69  E-value: 2.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 333 KLRKRGKIEEAVNAFEELVRKYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAptdLVKLslkrr 409
Cdd:COG1729   2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA---LLKL----- 73

                        90       100
                ....*....|....*....|....*.
gi 81913588 410 SERQQFLGHMRGSLLTLQRLVQLFPS 435
Cdd:COG1729  74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
430-531 6.93e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.24  E-value: 6.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 430 VQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESgDPgtDDGR 509
Cdd:COG0457   1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                        90       100
                ....*....|....*....|...
gi 81913588 510 FYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG0457  78 ALNNLGLALQALGRyEEALEDYD 100
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 324-510 2.28e-07

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 54.32  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   324 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAADL-PDAPTD-- 400
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   401 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLLGDN 453
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81913588   454 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTDDGRF 510
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
447-531 3.57e-07

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.63  E-value: 3.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 447 YLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 525
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                ....*.
gi 81913588 526 AYKWYE 531
Cdd:COG3063  78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 383-506 1.08e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 48.46  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 383 RAIETYQEAadLPDAPTDLVKLSLKRRSERQQflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEE 462
Cdd:COG4235   1 EAIARLRQA--LAANPNDAEGWLLLGRAYLRL--GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 81913588 463 VLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTD 506
Cdd:COG4235  77 ALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 321-504 1.57e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 51.62  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   321 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARY--GKAQCED-DL--AEKQrsnevLRRAIET-YQEAADL 394
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEKE-----LRKALSLgYPKNQVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   395 PDaptdLVKLSLKRRSerqqflghmrgslltLQRLVQLFPSDTTLKND--------LGVGYLLLGDNDSAKKVYEEVLNV 466
Cdd:TIGR02917  94 PL----LARAYLLQGK---------------FQQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 81913588   467 TPNDGFAKVHYGFILKAQNKISESIPYLKEgIESGDPG 504
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 331-404 1.65e-06

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 47.29  E-value: 1.65e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81913588 331 AEKLRKRGKIEEAVNAFEELVRKYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAPTDLVKL 404
Cdd:COG1729  37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 342-470 4.28e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 46.54  E-value: 4.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 342 EAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL-PDAPTDLVKLslkrrSERQQFLGHMR 420
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLL-------LGRAYLRLGRYDEALAAYEKALRLdPDNADALLDL-----AEALLAAGDTE 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 81913588 421 GSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPND 470
Cdd:COG4235  69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 328-398 9.78e-06

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 43.86  E-value: 9.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81913588   328 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL-PDAP 398
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
416-499 1.56e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.01  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 416 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKvYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLK 495
Cdd:COG3063   5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                ....
gi 81913588 496 EGIE 499
Cdd:COG3063  84 RALE 87
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 322-499 1.12e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.84  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   322 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL-PDAPTD 400
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALA-------LAQYYLGKGQLKKALAILNEAADAaPDSPEA 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   401 LVKL---------------SLKRRSERQ--QFLGHMR------------GSLLTLQRLVQLFPSDTTLKNDLGVGYLLLG 451
Cdd:TIGR02917 604 WLMLgraqlaagdlnkavsSFKKLLALQpdSALALLLladayavmknyaKAITSLKRALELKPDNTEAQIGLAQLLLAAK 683

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 81913588   452 DNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIE 499
Cdd:TIGR02917 684 RTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 316-436 1.34e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.49  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 316 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADL- 394
Cdd:COG4783  30 ALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLd 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 81913588 395 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSD 436
Cdd:COG4783 103 PEHPE-----AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 334-468 1.67e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.64  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 334 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAadlpdaptdlvklslkrrserq 413
Cdd:COG5010  64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYEKA---------------------- 114

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 81913588 414 qflghmrgslltlqrlVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTP 468
Cdd:COG5010 115 ----------------LALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 335-499 1.73e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.07  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   335 RKRGKIEEAVNAFEELVRKYPQSPRARYGKAqcedDLAEKQRSNEvlrRAIETYQEAADLpdAPTDL-VKLSLKRRSERQ 413
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALA----GLYLRTGNEE---EAVAWLEKAAEL--NPQEIePALALAQYYLGK 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   414 qflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPY 493
Cdd:TIGR02917 581 ---GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITS 657


                  ....*.
gi 81913588   494 LKEGIE 499
Cdd:TIGR02917 658 LKRALE 663
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 328-408 1.93e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 328 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL--PDAPTDLVKLS 405
Cdd:COG4235  55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                ...
gi 81913588 406 LKR 408
Cdd:COG4235 128 IAE 130
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 331-436 2.17e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 331 AEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADLpdAPTDLVKLSLKRRS 410
Cdd:COG4235  24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEELLERALAL--DPDNPEALYLLGLA 94

                        90       100
                ....*....|....*....|....*.
gi 81913588 411 ERQQflGHMRGSLLTLQRLVQLFPSD 436
Cdd:COG4235  95 AFQQ--GDYAEAIAAWQKLLALLPAD 118
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
321-473 2.64e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.98  E-value: 2.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 321 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAAdlpdaptd 400
Cdd:COG4785   3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQ-------- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81913588 401 lvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFA 473
Cdd:COG4785  75 ----LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 316-397 4.82e-04

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 42.56  E-value: 4.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 316 LLNKFDKTIKAElDAAEKLR------------------KRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCEDDLAEK 374
Cdd:COG4105 140 LINRYPDSEYAE-DAKKRIDelrdklarkelevaryylKRGAYVAAINRFQNVLEDYPDTPaveEALYLLVEAYYALGRY 218

                        90       100
                ....*....|....*....|...
gi 81913588 375 QRSNEVLRRAIETYQEAADLPDA 397
Cdd:COG4105 219 DEAQDAAAVLGKNYPDSPYLKDA 241
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 425-531 9.02e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 9.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 425 TLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDpg 504
Cdd:COG2956  30 LLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDP-- 107

                        90       100
                ....*....|....*....|....*...
gi 81913588 505 tDDGRFYFHLGDAMQRVGN-KEAYKWYE 531
Cdd:COG2956 108 -DDAEALRLLAEIYEQEGDwEKAIEVLE 134
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 341-416 1.12e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 41.40  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 341 EEAVNAFEELVRKYPQSPRARYGKA---QCEDDLAEK---------QRSNEV-----LRRAIETYQEAADLPDAPTDLVK 403
Cdd:COG4105 131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                        90
                ....*....|....*
gi 81913588 404 --LSLKRRSERQQFL 416
Cdd:COG4105 211 ayYALGRYDEAQDAA 225
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
334-469 2.97e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 334 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevlrraietYQEAadlpdaptdlvklslkrrserq 413
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLL---LLEQGR-----------YDEA---------------------- 45

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81913588 414 qflghmrgslLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPN 469
Cdd:COG3063  46 ----------IALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 316-366 3.05e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.05  E-value: 3.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 81913588 316 LLNKFDKTIKAE---LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQ 366
Cdd:COG1729  56 LLKRYPDSPKAPdalLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 316-394 4.35e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 39.71  E-value: 4.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81913588 316 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADL 394
Cdd:COG2956 170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLL 248
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 340-414 4.87e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 39.46  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   340 IEEAVNAFEELVRKYPQSPRARYGKAQ---CEDDLAEK---------QRSNEV-----LRRAIETYQEAADLPDAPTDLV 402
Cdd:TIGR03302 131 AREAFEAFQELIRRYPNSEYAPDAKKRmdyLRNRLAGKelyvarfylKRGAYVaainrFQTVVENYPDTPATEEALARLV 210

                          90
                  ....*....|....
gi 81913588   403 K--LSLKRRSERQQ 414
Cdd:TIGR03302 211 EayLKLGLTDLAQD 224
TPR_19 pfam14559
Tetratricopeptide repeat;
338-394 5.17e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.02  E-value: 5.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81913588   338 GKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADL 394
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRY 58
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 329-434 5.42e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 39.07  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588   329 DAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARygKAQCedDLAEKQRSNEVLRRAIETYQEAADL----PDAPTDLVKL 404
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE--QAQL--DLAYAYYKSGDYAEAIAAADRFIRLhpnhPDADYAYYLR 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 81913588   405 SL---KR--RSERQQflGHMRGSLLTLQRLVQLFP 434
Cdd:TIGR03302 114 GLsnyNQidRVDRDQ--TAAREAFEAFQELIRRYP 146
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 321-434 6.03e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 39.09  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81913588 321 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQC---EDDLAEkqrsnevlrrAIETYQEAADL 394
Cdd:COG4105  29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 81913588 395 ----PDAPTDLVKLSL-----KRRSERQQflGHMRGSLLTLQRLVQLFP 434
Cdd:COG4105  99 ypnsPNADYAYYLRGLsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYP 145
TPR_14 pfam13428
Tetratricopeptide repeat;
328-367 8.60e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 34.71  E-value: 8.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 81913588   328 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQC 367
Cdd:pfam13428   5 LALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
 
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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