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Conserved domains on  [gi|499972540|ref|WP_011653258|]
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MULTISPECIES: sugar transferase [Rhizobium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbaP_sugtrans super family cl37212
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
 23-233 8.73e-87

Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred.


The actual alignment was detected with superfamily member TIGR03022:

Pssm-ID: 274395 [Multi-domain]  Cd Length: 456  Bit Score: 264.22  E-value: 8.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   23 LHSSRPRAAgrssKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAE 102
Cdd:TIGR03022 250 LLLPSARLI----KRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTMVMNSDQVLEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  103 LLQNNPAARSEWEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMAVRPGL 182
Cdd:TIGR03022 326 LLAADPELRAEWEEYHKLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELYLRVRPGI 405

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499972540  183 TGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:TIGR03022 406 TGLWQVSGRNETTYDERVYLDVWYIKNWSLWLDIVILAKTIKVVLRRKGAY 456
 
Name Accession Description Interval E-value
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
 23-233 8.73e-87

Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred.


Pssm-ID: 274395 [Multi-domain]  Cd Length: 456  Bit Score: 264.22  E-value: 8.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   23 LHSSRPRAAgrssKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAE 102
Cdd:TIGR03022 250 LLLPSARLI----KRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTMVMNSDQVLEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  103 LLQNNPAARSEWEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMAVRPGL 182
Cdd:TIGR03022 326 LLAADPELRAEWEEYHKLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELYLRVRPGI 405

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499972540  183 TGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:TIGR03022 406 TGLWQVSGRNETTYDERVYLDVWYIKNWSLWLDIVILAKTIKVVLRRKGAY 456
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
 22-232 4.25e-79

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 240.41  E-value: 4.25e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  22 DLHSSRPRAAGRSSKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLA 101
Cdd:COG2148  125 SVRGPPLSGYQRVLKRLFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540 102 ELLqnnpaarseweetrKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGE-HIWAYMAVRP 180
Cdd:COG2148  205 AVF--------------KLKNDPRITRVGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEeEYRRRLLVKP 270

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499972540 181 GLTGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGS 232
Cdd:COG2148  271 GITGLAQVNGRNGETFEERVELDLYYIENWSLWLDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
 36-228 2.69e-77

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 230.71  E-value: 2.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   36 KRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAELlqnnpaarsewe 115
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLF------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  116 etrKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAE-ELPRYGEHIWAYMAVRPGLTGHWQ-TSGRND 193
Cdd:pfam02397  69 ---KLKNDPRITRVGRFLRKTSLDELPQLINVLKGDMSLVGPRPELPEfEYELYERDQRRRLSVKPGITGLAQvNGGRSE 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 499972540  194 VSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFS 228
Cdd:pfam02397 146 LSFEEKLELDLYYIENWSLWLDLKILLKTVKVVLK 180
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
 23-233 4.65e-67

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 214.10  E-value: 4.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  23 LHSSRPRAAGRSSKRALDLVIAVTALILLSPLLLIVAMIVKmSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAE 102
Cdd:PRK15204 267 IQNNLAKRSSRFLKRTFDIVCSIMILIIASPLMIYLWYKVT-RDGGPAIYGHQRVGRHGKLFPCYKFRSMVMNSQEVLKE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540 103 LLQNNPAARSEWEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMAVRPGL 182
Cdd:PRK15204 346 LLANDPIARAEWEKDFKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLMAKPGM 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499972540 183 TGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:PRK15204 426 TGLWQVSGRNDVDYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDGAY 476
 
Name Accession Description Interval E-value
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
 23-233 8.73e-87

Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred.


Pssm-ID: 274395 [Multi-domain]  Cd Length: 456  Bit Score: 264.22  E-value: 8.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   23 LHSSRPRAAgrssKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAE 102
Cdd:TIGR03022 250 LLLPSARLI----KRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTMVMNSDQVLEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  103 LLQNNPAARSEWEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMAVRPGL 182
Cdd:TIGR03022 326 LLAADPELRAEWEEYHKLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELYLRVRPGI 405

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499972540  183 TGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:TIGR03022 406 TGLWQVSGRNETTYDERVYLDVWYIKNWSLWLDIVILAKTIKVVLRRKGAY 456
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
 22-232 4.25e-79

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 240.41  E-value: 4.25e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  22 DLHSSRPRAAGRSSKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLA 101
Cdd:COG2148  125 SVRGPPLSGYQRVLKRLFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540 102 ELLqnnpaarseweetrKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGE-HIWAYMAVRP 180
Cdd:COG2148  205 AVF--------------KLKNDPRITRVGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEeEYRRRLLVKP 270

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499972540 181 GLTGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGS 232
Cdd:COG2148  271 GITGLAQVNGRNGETFEERVELDLYYIENWSLWLDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
 36-228 2.69e-77

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 230.71  E-value: 2.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   36 KRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAELlqnnpaarsewe 115
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLF------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  116 etrKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAE-ELPRYGEHIWAYMAVRPGLTGHWQ-TSGRND 193
Cdd:pfam02397  69 ---KLKNDPRITRVGRFLRKTSLDELPQLINVLKGDMSLVGPRPELPEfEYELYERDQRRRLSVKPGITGLAQvNGGRSE 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 499972540  194 VSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFS 228
Cdd:pfam02397 146 LSFEEKLELDLYYIENWSLWLDLKILLKTVKVVLK 180
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
 22-233 2.34e-73

exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.


Pssm-ID: 274398 [Multi-domain]  Cd Length: 445  Bit Score: 229.40  E-value: 2.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   22 DLHSSRPRAAGRSSKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNAsaqla 101
Cdd:TIGR03025 244 SLSNFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDA----- 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  102 ellqnnpAARSEWeeTRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMA---V 178
Cdd:TIGR03025 319 -------EEGGGP--VQATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLrhkV 389

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499972540  179 RPGLTGHWQTSGRNDVS-YEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:TIGR03025 390 KPGITGWAQVSGRGETStMEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
 23-233 4.65e-67

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 214.10  E-value: 4.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  23 LHSSRPRAAGRSSKRALDLVIAVTALILLSPLLLIVAMIVKmSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAE 102
Cdd:PRK15204 267 IQNNLAKRSSRFLKRTFDIVCSIMILIIASPLMIYLWYKVT-RDGGPAIYGHQRVGRHGKLFPCYKFRSMVMNSQEVLKE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540 103 LLQNNPAARSEWEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYMAVRPGL 182
Cdd:PRK15204 346 LLANDPIARAEWEKDFKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLMAKPGM 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499972540 183 TGHWQTSGRNDVSYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:PRK15204 426 TGLWQVSGRNDVDYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDGAY 476
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
 32-233 1.89e-56

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 185.87  E-value: 1.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   32 GRSSKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQlaellqnnpaar 111
Cdd:TIGR03023 256 NRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGD------------ 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  112 sewEETRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYM---AVRPGLTGHWQT 188
Cdd:TIGR03023 324 ---GVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMlrhKVKPGITGWAQV 400

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499972540  189 SG-RNDV----SYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:TIGR03023 401 NGlRGETdtleKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
 32-223 9.64e-38

sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the family of bacterial sugar transferases (pfam02397). Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria (notable exceptions appear to include Magnetococcus sp. MC-1 and Myxococcus xanthus DK 1622 ). These genes are generally found near one or more of the PrsK, PrsR or PrsT genes that have been related to the PEP-CTERM system by phylogenetic profiling methods. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species. These proteins are homologs of the EpsB protein found in Methylobacillus sp. strain 12S, which is also associated with a PEP-CTERM system, but of a distinct type. A name which appears attached to a number of genes (by transitive annotation) in this family is "undecaprenyl-phosphate galactose phosphotransferase", which comes from relatively distant characterized enterobacterial homologs, and is considerably more specific than warranted from the currently available evidence.


Pssm-ID: 274390 [Multi-domain]  Cd Length: 442  Bit Score: 136.36  E-value: 9.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540   32 GRSSKRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKTNASAQLAELLQnnpaar 111
Cdd:TIGR03013 252 RRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAVWAQ------ 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  112 seweetrklKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRP-------ITAEELPRYGE-HiwaymAVRPGLT 183
Cdd:TIGR03013 326 ---------KDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPerpefveKLSEEIPYYNErH-----RVKPGIT 391

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 499972540  184 GHWQtsgrndVSYEY---------RVSLDVHYLNNWSLGRDFIIIAKTI 223
Cdd:TIGR03013 392 GWAQ------IKYPYgasvadakeKLRYDLYYIKNMSLLLDLIILIQTF 434
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
 36-233 5.63e-32

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 121.37  E-value: 5.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540  36 KRALDLVIAVTALILLSPLLLIVAMIVKMSDRGPVFYSHTRIGVGGAPFGCLKFRTMKtnasaqlaeLLQNNPAArsewe 115
Cdd:PRK10124 273 KRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMK---------VMENDKVV----- 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499972540 116 eTRKLKDDPRITAVGDILRRSSIDELPQLINIVRGDMSLVGPRPITAEELPRYGEHIWAYM---AVRPGLTGHWQTSG-R 191
Cdd:PRK10124 339 -TQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMlrhKVKPGITGWAQINGwR 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 499972540 192 NDV----SYEYRVSLDVHYLNNWSLGRDFIIIAKTIPALFSQRGSY 233
Cdd:PRK10124 418 GETdtleKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
 
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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