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Conserved domains on  [gi|564117499|gb|AHB69820|]
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putative UDP-glucose lipid carrier transferase [Cronobacter malonaticus]

Protein Classification

undecaprenyl-phosphate glucose phosphotransferase( domain architecture ID 11484584)

undecaprenyl-phosphate glucose phosphotransferase 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); also possesses a weak galactose-1-P transferase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-436 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


:

Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 912.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   1 MFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESP 80
Cdd:PRK10124  28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNNDFDTQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  81 FRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTG 160
Cdd:PRK10124 108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGGVSND 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 161 WAGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVPLYDTPLSG 240
Cdd:PRK10124 188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 241 INRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPR 320
Cdd:PRK10124 268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPR 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 321 VTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRGETDTLEKME 400
Cdd:PRK10124 348 VTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDTLEKME 427
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 564117499 401 KRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:PRK10124 428 KRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-436 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 912.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   1 MFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESP 80
Cdd:PRK10124  28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNNDFDTQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  81 FRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTG 160
Cdd:PRK10124 108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGGVSND 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 161 WAGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVPLYDTPLSG 240
Cdd:PRK10124 188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 241 INRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPR 320
Cdd:PRK10124 268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPR 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 321 VTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRGETDTLEKME 400
Cdd:PRK10124 348 VTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDTLEKME 427
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 564117499 401 KRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:PRK10124 428 KRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
1-436 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: 619.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499    1 MFVGLWVVCRIN----ELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMS-LVFSAGLMAFNP 75
Cdd:TIGR03023   7 IALALLLAYLLRfgsrGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTfLILALLAFLLKT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   76 DFESPFRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPG 155
Cdd:TIGR03023  87 GTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  156 GVPTGW---AGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVP 232
Cdd:TIGR03023 167 RTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVIS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  233 LYDTPLSGINRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVK 312
Cdd:TIGR03023 247 LRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVT 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  313 QATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRGE 392
Cdd:TIGR03023 327 QATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGE 406
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 564117499  393 TDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:TIGR03023 407 TDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
99-435 3.46e-114

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 337.48  E-value: 3.46e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  99 RSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTGwAGNLEQLVEDARMGKIH 178
Cdd:COG2148    2 LRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLL-GDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 179 NVYIAMSMSEEAQMKKLVRQLSDTTCSvmlipdvftFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASMIL 258
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 259 LLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQATQNDPRVTKVGNFLRRTSLDELP 337
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 338 QFINVLTGEMSIVGPRPHAVAHNEQYRAliQGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSVWL 417
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 564117499 418 DIKIVFLTVFKGFVNKAA 435
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
246-430 1.77e-99

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: 294.65  E-value: 1.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  246 KRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPRVTKVG 325
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  326 NFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHneQYRALIQGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEF 405
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 564117499  406 DLEYIREWSVWLDIKIVFLTVFKGF 430
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-436 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 912.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   1 MFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESP 80
Cdd:PRK10124  28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNNDFDTQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  81 FRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTG 160
Cdd:PRK10124 108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGGVSND 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 161 WAGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVPLYDTPLSG 240
Cdd:PRK10124 188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 241 INRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPR 320
Cdd:PRK10124 268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPR 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 321 VTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRGETDTLEKME 400
Cdd:PRK10124 348 VTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDTLEKME 427
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 564117499 401 KRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:PRK10124 428 KRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
1-436 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: 619.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499    1 MFVGLWVVCRIN----ELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMS-LVFSAGLMAFNP 75
Cdd:TIGR03023   7 IALALLLAYLLRfgsrGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTfLILALLAFLLKT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   76 DFESPFRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPG 155
Cdd:TIGR03023  87 GTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  156 GVPTGW---AGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVP 232
Cdd:TIGR03023 167 RTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVIS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  233 LYDTPLSGINRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVK 312
Cdd:TIGR03023 247 LRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGVT 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  313 QATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRGE 392
Cdd:TIGR03023 327 QATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQVNGLRGE 406
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 564117499  393 TDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:TIGR03023 407 TDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
1-436 0e+00

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: 531.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499    1 MFVGLWVVCRINELPFFYMHLLMALTTLVVFqmIGGITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESP 80
Cdd:TIGR03025  12 LLAFLLLGLGLLPPPDFYSLLLLLLLLLFLI--LFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFKSFDFS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   81 FRVFFAWYLLTGAGMVICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTG 160
Cdd:TIGR03025  90 RLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDDRPSDRVEVA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  161 ---WAGNLEQLVEDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVPLYDTP 237
Cdd:TIGR03025 170 glpVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLSNFP 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  238 LSGINRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQATQ 316
Cdd:TIGR03025 250 LSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGPVQATK 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  317 NDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGwRGETDTl 396
Cdd:TIGR03025 330 NDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSG-RGETST- 407
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 564117499  397 ekMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 436
Cdd:TIGR03025 408 --MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
99-435 3.46e-114

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 337.48  E-value: 3.46e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  99 RSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDPEPGGVPTGwAGNLEQLVEDARMGKIH 178
Cdd:COG2148    2 LRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLL-GDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 179 NVYIAMSMSEEAQMKKLVRQLSDTTCSvmlipdvftFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASMIL 258
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 259 LLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQATQNDPRVTKVGNFLRRTSLDELP 337
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 338 QFINVLTGEMSIVGPRPHAVAHNEQYRAliQGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSVWL 417
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 564117499 418 DIKIVFLTVFKGFVNKAA 435
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
246-430 1.77e-99

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: 294.65  E-value: 1.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  246 KRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPRVTKVG 325
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  326 NFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHneQYRALIQGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEF 405
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 564117499  406 DLEYIREWSVWLDIKIVFLTVFKGF 430
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
97-426 1.61e-74

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: 240.34  E-value: 1.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   97 ICRSAIRFGAGWLRNrgyntrrVAIAGAQPVGQQLAESFRNEPWLGFEVVGIY------HDPEPGGVPtgWAGNLEQLVE 170
Cdd:TIGR03022 113 LVRKLLSRRGWWGRP-------AVIIGAGQNAAILYRALQSNPQLGLRPLAVVdtdpaaSGRLLTGLP--VVGADDALRL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  171 DARMGKIHnVYIAMSMSEEAQMKKLVRQLSDTTCS-VMLIPDVFTFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLE 249
Cdd:TIGR03022 184 YARTRYAY-VIVAMPGTQAEDMARLVRKLGALHFRnVLIVPSLFGLPNLWISPRFIGGVLGLRVRNNLLLPSARLIKRTL 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  250 DIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMrVMENDKVVKQ---------------- 313
Cdd:TIGR03022 263 DLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTM-VMNSDQVLEEllaadpelraeweeyh 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  314 ATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYmlrHKVKPGITGWAQINGwRGET 393
Cdd:TIGR03022 342 KLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELY---LRVRPGITGLWQVSG-RNET 417
                         330       340       350
                  ....*....|....*....|....*....|...
gi 564117499  394 DtlekMEKRIEFDLEYIREWSVWLDIKIVFLTV 426
Cdd:TIGR03022 418 T----YDERVYLDVWYIKNWSLWLDIVILAKTI 446
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
12-426 9.74e-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: 201.08  E-value: 9.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   12 NELPFFYMHLLMALTTLVVF----QMIGGITDFYRSWRGVKISTELLLLLqnwtMSLVFSAGLMAF----NPDFESPFRV 83
Cdd:TIGR03013  20 YQIGMFSLLSLVPLAQLVTFalvvIISAIALGLYNVDLREDFRGIIARLA----ISLLVSFLALSFifyfYPEFYLGRGL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   84 FFAWYLLTGAGMVICRSAIRFgagWLRNRGYNtRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIYHDP-EPGGVPT-GW 161
Cdd:TIGR03013  96 LALAIVLAGSLVLLSRLFFLK---ILGLQGLK-RRILVLGTGPRAREIARLRRSSDRRGHEIVGFVPLPdEPAYVPSeHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  162 AGNLEQLVEDARMGKIHNVYIAMSmseEAQMKKLVRQLSDTTCSVMLIPDVFTFNILHSRLDDVNGV-PVVPLYDTPL-- 238
Cdd:TIGR03013 172 IENGDGLVEYVLRHRIDEIVIALD---ERRGSLPVDELLECKLSGIEVVDAPSFFERETGKIAIDLIyPSWLIFSNGFrn 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  239 SGINRVLKRLEDIVLASMILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQND 318
Cdd:TIGR03013 249 SSLRRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAVWAQKDD 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  319 PRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGWRG--ETDTL 396
Cdd:TIGR03013 329 PRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGasVADAK 408
                         410       420       430
                  ....*....|....*....|....*....|
gi 564117499  397 EKMekriEFDLEYIREWSVWLDIKIVFLTV 426
Cdd:TIGR03013 409 EKL----RYDLYYIKNMSLLLDLIILIQTF 434
CoA_binding_3 pfam13727
CoA-binding domain;
37-210 7.66e-47

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 158.97  E-value: 7.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499   37 ITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESpfRVFFAWYLLTGAGMVICRSAIRF--GAGWLRNRGY 114
Cdd:pfam13727   2 AFGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIFS--RLWLAYWAVSGIALLILSRLLLRavLRRYRRHGRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  115 NTRRVAIAGAQPVGQQLaesfRNEPWLGFEVVGIYHDPEPGGVPTG----WAGNLEQLVEDARMGKIHNVYIAMSMSEEA 190
Cdd:pfam13727  80 NRRVVAVGGGLELARQI----RANPWLGFRVVGVFDDRDDDRVPEVagvpVLGNLADLVEYVRETRVDEVYLALPLSAEA 155
                         170       180
                  ....*....|....*....|
gi 564117499  191 QMKKLVRQLSDTTCSVMLIP 210
Cdd:pfam13727 156 RILRLVKELRDDPVNIRLIP 175
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
52-426 1.04e-43

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 159.40  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  52 ELLLLLQNWTMSLVFSAGLMAFNPDFESPFRVFFAWYLltgagMVICRSAIRFGAGWLRNR-GYNTRRVAIAGAQPVGQQ 130
Cdd:PRK15204  86 ELKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFCWTF-----ALILVPFFRALTKHLLNKlGIWKKKTIILGSGQNARG 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 131 LAESFRNEPWLGFEVVGIYH----DPEPGGVPTGWAGNLeqLVEDARMGKIHNVyIAMSMSEEAQMKKLVRQLSDTTC-S 205
Cdd:PRK15204 161 AYSALQSEEMMGFDVIAFFDtdasDAEINMLPVIKDTEI--IWDLNRTGDVHYI-LAYEYTELEKTHFWLRELSKHHCrS 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 206 VMLIPDVFTfnilhsrlddvngvpvVPLYDTPLSGI------------------NRVLKRLEDIVLASMILLLISPVLCC 267
Cdd:PRK15204 238 VTVVPSFRG----------------LPLYNTDMSFIfshevmllriqnnlakrsSRFLKRTFDIVCSIMILIIASPLMIY 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 268 IAVAVKLSSpGPIIFRQTRYGMDGKPIMVWKFRSMrVMENDKVVKQ----------------ATQNDPRVTKVGNFLRRT 331
Cdd:PRK15204 302 LWYKVTRDG-GPAIYGHQRVGRHGKLFPCYKFRSM-VMNSQEVLKEllandpiaraewekdfKLKNDPRITAVGRFIRKT 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499 332 SLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLrhkVKPGITGWAQINGwRGETDtlekMEKRIEFDLEYIR 411
Cdd:PRK15204 380 SLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-RNDVD----YDTRVYFDSWYVK 451
                        410
                 ....*....|....*
gi 564117499 412 EWSVWLDIKIVFLTV 426
Cdd:PRK15204 452 NWTLWNDIAILFKTA 466
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
96-211 4.90e-25

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: 99.23  E-value: 4.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564117499  96 VICRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAESFRNEPWLGFEVVGIY------HDPEPGGVPtgWAGNLEQLV 169
Cdd:COG1086    1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVdddpdkRGRRIEGVP--VLGTLDDLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564117499 170 EDARMGKIHNVYIAMSMSEEAQMKKLVRQLSDTTCSVMLIPD 211
Cdd:COG1086   79 ELVRRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPD 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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