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Conserved domains on  [gi|2095993166|gb|UAW99441|]
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undecaprenyl-phosphate glucose phosphotransferase [Pseudomonas nanhaiensis]

Protein Classification

sugar transferase( domain architecture ID 11496316)

sugar transferase similar to Xanthomonas campestris UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase that catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
37-471 0e+00

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: 593.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  37 YWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLELRKVASNWAATFAAVFAVDYFLLPSRTLPNTDGVLWF 116
Cdd:TIGR03023  20 GSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALLAFLLKTGTEFSRLWLLLWF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 117 TLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGGtsvrLPI 196
Cdd:TIGR03023 100 LLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDARTSVRG----VPV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 197 NGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTASVYLIPDVFVFDLLHARSESINGLPSISIFDTPMDGA 276
Cdd:TIGR03023 176 LGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRDSPLDGW 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 277 SRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARI 356
Cdd:TIGR03023 256 NRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVTQATRNDPRV 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 357 TRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRKLINGYMLRHKVKPGITGWAQVNGWRGETDTLDKMAK 436
Cdd:TIGR03023 336 TRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGETDTLEKMEK 415
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2095993166 437 RIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:TIGR03023 416 RVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
37-471 0e+00

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: 593.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  37 YWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLELRKVASNWAATFAAVFAVDYFLLPSRTLPNTDGVLWF 116
Cdd:TIGR03023  20 GSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALLAFLLKTGTEFSRLWLLLWF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 117 TLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGGtsvrLPI 196
Cdd:TIGR03023 100 LLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDARTSVRG----VPV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 197 NGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTASVYLIPDVFVFDLLHARSESINGLPSISIFDTPMDGA 276
Cdd:TIGR03023 176 LGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRDSPLDGW 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 277 SRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARI 356
Cdd:TIGR03023 256 NRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVTQATRNDPRV 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 357 TRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRKLINGYMLRHKVKPGITGWAQVNGWRGETDTLDKMAK 436
Cdd:TIGR03023 336 TRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGETDTLEKMEK 415
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2095993166 437 RIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:TIGR03023 416 RVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-471 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 545.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166   1 MPRYQRGILHSREPLLSLLHRVLDLAFIAAAFFATLYWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLEL 80
Cdd:PRK10124    1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  81 RKVASNWAATFAAVFAVDYFLlPSRTLPNTDGVLWFTLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLA 160
Cdd:PRK10124   81 ALLLQNWTLSLIFSAGLVAFN-NDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 161 NTIMKAPWMGLDLLGFYDDmsvePVSLGgtsVRLPINGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTAS 240
Cdd:PRK10124  160 ESFRNEPWLGFEVVGVYHD----PKPGG---VSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 241 VYLIPDVFVFDLLHARSESINGLPSISIFDTPMDGASRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQ 320
Cdd:PRK10124  233 VLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 321 RYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARITRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRK 400
Cdd:PRK10124  313 RYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQ 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095993166 401 LINGYMLRHKVKPGITGWAQVNGWRGETDTLDKMAKRIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:PRK10124  393 LIEGYMLRHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
137-470 1.62e-108

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 324.38  E-value: 1.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 137 MRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGGTSVRLPINGNMANLIAEAREGRIDKVY 216
Cdd:COG2148     4 LLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVVIIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 217 ITLPMRAEEKIKWLVDALSDTtasvylipdVFVFDLLHARSESINGLPSISIFDTPMDGASRVIKRMEDVVLSSLILALI 296
Cdd:COG2148    84 LLALLLRELLLLLLLLLLRLL---------GVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 297 ALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVM-EDGDDVVQATRGDARITRLGAFLRRTSLDELPQFV 375
Cdd:COG2148   155 SPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLW 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 376 NVLLGDMSIVGPRPHAVAHNEEYRKLinGYMLRHKVKPGITGWAQVNGWRGETdtldkMAKRIECDLDYIRHWSLWLDLK 455
Cdd:COG2148   235 NVLKGDMSLVGPRPELPEEVELYEEE--EYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLK 307
                         330
                  ....*....|....*
gi 2095993166 456 IVFMTVFKGFVNPNA 470
Cdd:COG2148   308 ILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
281-465 2.06e-95

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: 285.41  E-value: 2.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 281 KRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARITRLG 360
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 361 AFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHneEYRKLINGYMLRHKVKPGITGWAQVNGWRGETDtldkMAKRIEC 440
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 2095993166 441 DLDYIRHWSLWLDLKIVFMTVFKGF 465
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
37-471 0e+00

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: 593.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  37 YWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLELRKVASNWAATFAAVFAVDYFLLPSRTLPNTDGVLWF 116
Cdd:TIGR03023  20 GSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALLAFLLKTGTEFSRLWLLLWF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 117 TLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGGtsvrLPI 196
Cdd:TIGR03023 100 LLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDARTSVRG----VPV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 197 NGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTASVYLIPDVFVFDLLHARSESINGLPSISIFDTPMDGA 276
Cdd:TIGR03023 176 LGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRDSPLDGW 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 277 SRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARI 356
Cdd:TIGR03023 256 NRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVTQATRNDPRV 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 357 TRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRKLINGYMLRHKVKPGITGWAQVNGWRGETDTLDKMAK 436
Cdd:TIGR03023 336 TRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGETDTLEKMEK 415
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2095993166 437 RIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:TIGR03023 416 RVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-471 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 545.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166   1 MPRYQRGILHSREPLLSLLHRVLDLAFIAAAFFATLYWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLEL 80
Cdd:PRK10124    1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  81 RKVASNWAATFAAVFAVDYFLlPSRTLPNTDGVLWFTLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLA 160
Cdd:PRK10124   81 ALLLQNWTLSLIFSAGLVAFN-NDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 161 NTIMKAPWMGLDLLGFYDDmsvePVSLGgtsVRLPINGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTAS 240
Cdd:PRK10124  160 ESFRNEPWLGFEVVGVYHD----PKPGG---VSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 241 VYLIPDVFVFDLLHARSESINGLPSISIFDTPMDGASRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQ 320
Cdd:PRK10124  233 VLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 321 RYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARITRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRK 400
Cdd:PRK10124  313 RYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQ 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095993166 401 LINGYMLRHKVKPGITGWAQVNGWRGETDTLDKMAKRIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:PRK10124  393 LIEGYMLRHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
36-471 8.83e-165

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: 472.46  E-value: 8.83e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  36 LYWNDTPLRQEYLLCVTGSLFLFYLISDFSQLYGSWRGEHSLLELRKVASNWAATFAAVFAVDYFL----LPSRTLpntd 111
Cdd:TIGR03025  18 LGLGLLPPPDFYSLLLLLLLLLFLILFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFksfdFSRLVL---- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 112 gVLWFTLALVGLASHRVVLRLVVRRMRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDmsvePVSLGGTS 191
Cdd:TIGR03025  94 -LLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDD----RPSDRVEV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 192 VRLPINGNMANLIAEAREGRIDKVYITLPMRAEEKIKWLVDALSDTTASVYLIPDVFVFDLLHARSESINGLPSISIFDT 271
Cdd:TIGR03025 169 AGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLSNF 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 272 PMDGASRVIKRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVM-EDGDDVVQAT 350
Cdd:TIGR03025 249 PLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGPVQAT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 351 RGDARITRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRKLINGYMLRHKVKPGITGWAQVNGwRGETDT 430
Cdd:TIGR03025 329 KNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSG-RGETST 407
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 2095993166 431 ldkMAKRIECDLDYIRHWSLWLDLKIVFMTVFKGFVNPNAY 471
Cdd:TIGR03025 408 ---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
137-470 1.62e-108

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 324.38  E-value: 1.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 137 MRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGGTSVRLPINGNMANLIAEAREGRIDKVY 216
Cdd:COG2148     4 LLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVVIIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 217 ITLPMRAEEKIKWLVDALSDTtasvylipdVFVFDLLHARSESINGLPSISIFDTPMDGASRVIKRMEDVVLSSLILALI 296
Cdd:COG2148    84 LLALLLRELLLLLLLLLLRLL---------GVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 297 ALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVM-EDGDDVVQATRGDARITRLGAFLRRTSLDELPQFV 375
Cdd:COG2148   155 SPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLW 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 376 NVLLGDMSIVGPRPHAVAHNEEYRKLinGYMLRHKVKPGITGWAQVNGWRGETdtldkMAKRIECDLDYIRHWSLWLDLK 455
Cdd:COG2148   235 NVLKGDMSLVGPRPELPEEVELYEEE--EYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLK 307
                         330
                  ....*....|....*
gi 2095993166 456 IVFMTVFKGFVNPNA 470
Cdd:COG2148   308 ILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
281-465 2.06e-95

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: 285.41  E-value: 2.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 281 KRMEDVVLSSLILALIALPMLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARITRLG 360
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 361 AFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHneEYRKLINGYMLRHKVKPGITGWAQVNGWRGETDtldkMAKRIEC 440
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 2095993166 441 DLDYIRHWSLWLDLKIVFMTVFKGF 465
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
145-461 5.40e-60

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: 203.00  E-value: 5.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 145 RSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFyddmsvepVSLGGTSVRLP---INGNMANLIAEAREGRIDKVYITLpm 221
Cdd:TIGR03013 125 RRILVLGTGPRAREIARLRRSSDRRGHEIVGF--------VPLPDEPAYVPsehVIENGDGLVEYVLRHRIDEIVIAL-- 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 222 rAEEKIKWLVDALSDTTASVYLIPDVFVFDLLHARSESINGL-PSISIFDTPMDGAS--RVIKRMEDVVlSSLILALIAL 298
Cdd:TIGR03013 195 -DERRGSLPVDELLECKLSGIEVVDAPSFFERETGKIAIDLIyPSWLIFSNGFRNSSlrRITKRSFDVV-ASLILLILTL 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 299 P-MLLIGLGVKLTSPGPALFRQQRYGIDGKPISVWKFRSMRVMEDGDDVVQATRGDARITRLGAFLRRTSLDELPQFVNV 377
Cdd:TIGR03013 273 PvMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAVWAQKDDPRVTRVGRFLRKTRIDELPQIFNV 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 378 LLGDMSIVGPRPHAVAHNEEYRKLINGYMLRHKVKPGITGWAQVNGWRG--ETDTLDKMakriECDLDYIRHWSLWLDLK 455
Cdd:TIGR03013 353 LRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGasVADAKEKL----RYDLYYIKNMSLLLDLI 428

                  ....*.
gi 2095993166 456 IVFMTV 461
Cdd:TIGR03013 429 ILIQTF 434
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
141-461 5.47e-37

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 141.68  E-value: 5.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 141 GFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSLGgtsvrLPINGNMANLIAEAREGRIDKVYITLP 220
Cdd:PRK15204  143 GIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINM-----LPVIKDTEIIWDLNRTGDVHYILAYEY 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 221 MRAEEKIKWLVDALSDTTASVYLIPdvfvfdllharseSINGLPsisIFDTPMD------------------GASRVIKR 282
Cdd:PRK15204  218 TELEKTHFWLRELSKHHCRSVTVVP-------------SFRGLP---LYNTDMSfifshevmllriqnnlakRSSRFLKR 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 283 MEDVVLSSLILaLIALPmLLIGLGVKLTSPG-PALFRQQRYGIDGKPISVWKFRSMrVME---------DGDDVVQAT-- 350
Cdd:PRK15204  282 TFDIVCSIMIL-IIASP-LMIYLWYKVTRDGgPAIYGHQRVGRHGKLFPCYKFRSM-VMNsqevlkellANDPIARAEwe 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 351 -----RGDARITRLGAFLRRTSLDELPQFVNVLLGDMSIVGPRPHAVAHNEEYRKLINGYMLrhkVKPGITGWAQVNGwR 425
Cdd:PRK15204  359 kdfklKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-R 434
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2095993166 426 GETDtldkMAKRIECDLDYIRHWSLWLDLKIVFMTV 461
Cdd:PRK15204  435 NDVD----YDTRVYFDSWYVKNWTLWNDIAILFKTA 466
CoA_binding_3 pfam13727
CoA-binding domain;
67-245 1.60e-21

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 91.56  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166  67 LYGSWRGEHSLLELRKVASNWAATFAAVFAVDYFLLP--SRTLPntdgVLWFTLALVGL-ASHRVVLRLVVRRMRSRGFN 143
Cdd:pfam13727   5 VYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDifSRLWL----AYWAVSGIALLiLSRLLLRAVLRRYRRHGRNN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 144 TRSVAIAGagplGQRLANTIMKAPWMGLDLLGFYDDMSVEPVSlggTSVRLPINGNMANLIAEAREGRIDKVYITLPMRA 223
Cdd:pfam13727  81 RRVVAVGG----GLELARQIRANPWLGFRVVGVFDDRDDDRVP---EVAGVPVLGNLADLVEYVRETRVDEVYLALPLSA 153
                         170       180
                  ....*....|....*....|..
gi 2095993166 224 EEKIKWLVDALSDTTASVYLIP 245
Cdd:pfam13727 154 EARILRLVKELRDDPVNIRLIP 175
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
137-246 1.79e-21

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 89.60  E-value: 1.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095993166 137 MRSRGFNTRSVAIAGAGPLGQRLANTIMKAPWMGLDLLGFYDDmsvEPVSLGGTSVRLPINGNMANLIAEAREGRIDKVY 216
Cdd:COG1086    14 LRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDD---DPDKRGRRIEGVPVLGTLDDLPELVRRLGVDEVI 90
                          90       100       110
                  ....*....|....*....|....*....|
gi 2095993166 217 ITLPMRAEEKIKWLVDALSDTTASVYLIPD 246
Cdd:COG1086    91 IALPSASRERLRELLEQLEDLGVKVKIVPD 120
 
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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