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Conserved domains on  [gi|490521324|ref|WP_004386776|]
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MULTISPECIES: undecaprenyl-phosphate glucose phosphotransferase [Cronobacter]

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
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


:

Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 945.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   2 TNLKKRERAKTNASLISLVQRFSDITIMFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  82 LLLLQNWTMSLVFSAGLMAFNPDFESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 162 SFRNEPWLGFEVVGIYHDPEPGGVPTGWAGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 242 TFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 322 IMVWKFRSMRVMENDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490521324 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 945.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   2 TNLKKRERAKTNASLISLVQRFSDITIMFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  82 LLLLQNWTMSLVFSAGLMAFNPDFESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 162 SFRNEPWLGFEVVGIYHDPEPGGVPTGWAGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 242 TFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 322 IMVWKFRSMRVMENDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490521324 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
23-464 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: 601.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   23 FSDITIMFVGLWVVCRIN----ELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMS-LVFSAG 97
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRfgsrGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTfLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   98 LMAFNPDFESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIY 177
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  178 HDPEPGGVPTGW---AGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVFTFNILHSRLDDVN 254
Cdd:TIGR03023 161 DDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  255 GVPVVPLYDTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVME 334
Cdd:TIGR03023 241 GLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  335 NDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQI 414
Cdd:TIGR03023 321 EGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQV 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 490521324  415 NGWRGETDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03023 401 NGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
127-463 6.28e-107

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 320.14  E-value: 6.28e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 127 RSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIYHDPEPGGVPTGwAGNLEQLVEDARTGKIH 206
Cdd:COG2148    2 LRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLL-GDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 207 NVYIAMSMSEEAQMKKLVRELSDTTCSvmlipdvftFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASLIL 286
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 287 LLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQATQNDPRVTKVGNFLRRTSLDELP 365
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 366 QFINVLTGEMSIVGPRPHAVAHNEQYRAliQGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSVWL 445
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 490521324 446 DIKIVFLTVFKGFVNKAA 463
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
274-458 7.57e-91

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: 273.47  E-value: 7.57e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  274 KRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPRVTKVG 353
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  354 NFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHneQYRALIQGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEF 433
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 490521324  434 DLEYIREWSVWLDIKIVFLTVFKGF 458
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 945.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   2 TNLKKRERAKTNASLISLVQRFSDITIMFVGLWVVCRINELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  82 LLLLQNWTMSLVFSAGLMAFNPDFESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLAD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 162 SFRNEPWLGFEVVGIYHDPEPGGVPTGWAGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 242 TFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 322 IMVWKFRSMRVMENDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490521324 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
23-464 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: 601.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   23 FSDITIMFVGLWVVCRIN----ELPFFYMHLLMALTTLVVFQMIGGITDFYRSWRGVKISTELLLLLQNWTMS-LVFSAG 97
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRfgsrGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTfLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   98 LMAFNPDFESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIY 177
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  178 HDPEPGGVPTGW---AGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVFTFNILHSRLDDVN 254
Cdd:TIGR03023 161 DDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  255 GVPVVPLYDTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVME 334
Cdd:TIGR03023 241 GLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  335 NDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQI 414
Cdd:TIGR03023 321 EGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQV 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 490521324  415 NGWRGETDTLEKMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03023 401 NGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
26-464 1.93e-179

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: 509.44  E-value: 1.93e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   26 ITIMFVGLWVVCRINELPFFYMHLLMALTTLVVFqmIGGITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDF 105
Cdd:TIGR03025   9 LAFLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLI--LFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFKSF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  106 ESPFRVYLAWYLLTGAGMVMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIYHDPEPGGV 185
Cdd:TIGR03025  87 DFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDDRPSDRV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  186 PTG---WAGNLEQLVEDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPDVFTFNILHSRLDDVNGVPVVPLY 262
Cdd:TIGR03025 167 EVAglpVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  263 DTPLSGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQ 341
Cdd:TIGR03025 247 NFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGPVQ 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  342 ATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGITGWAQINGwRGET 421
Cdd:TIGR03025 327 ATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSG-RGET 405
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 490521324  422 DTlekMEKRIEFDLEYIREWSVWLDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03025 406 ST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
127-463 6.28e-107

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 320.14  E-value: 6.28e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 127 RSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIYHDPEPGGVPTGwAGNLEQLVEDARTGKIH 206
Cdd:COG2148    2 LRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLL-GDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 207 NVYIAMSMSEEAQMKKLVRELSDTTCSvmlipdvftFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLEDIVLASLIL 286
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 287 LLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVM-ENDKVVKQATQNDPRVTKVGNFLRRTSLDELP 365
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 366 QFINVLTGEMSIVGPRPHAVAHNEQYRAliQGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSVWL 445
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 490521324 446 DIKIVFLTVFKGFVNKAA 463
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
274-458 7.57e-91

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: 273.47  E-value: 7.57e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  274 KRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMRVMENDKVVKQATQNDPRVTKVG 353
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  354 NFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHneQYRALIQGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEF 433
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 490521324  434 DLEYIREWSVWLDIKIVFLTVFKGF 458
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
126-454 5.74e-68

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: 224.16  E-value: 5.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  126 CRSAIRFGAGWLRNrgyntrrVAIAGAQPVGQQLADSFRNEPWLGFEVVGIY------HDPEPGGVPtgWAGNLEQLVED 199
Cdd:TIGR03022 114 VRKLLSRRGWWGRP-------AVIIGAGQNAAILYRALQSNPQLGLRPLAVVdtdpaaSGRLLTGLP--VVGADDALRLY 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  200 ARTGKIHnVYIAMSMSEEAQMKKLVRELSDTTCS-VMLIPDVFTFNILHSRLDDVNGVPVVPLYDTPLSGINRVLKRLED 278
Cdd:TIGR03022 185 ARTRYAY-VIVAMPGTQAEDMARLVRKLGALHFRnVLIVPSLFGLPNLWISPRFIGGVLGLRVRNNLLLPSARLIKRTLD 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  279 IVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFRSMrVMENDKVVKQ----------------A 342
Cdd:TIGR03022 264 LVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTM-VMNSDQVLEEllaadpelraeweeyhK 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  343 TQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYmlrHKVKPGITGWAQINGwRGETD 422
Cdd:TIGR03022 343 LRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALELY---LRVRPGITGLWQVSG-RNETT 418
                         330       340       350
                  ....*....|....*....|....*....|..
gi 490521324  423 tlekMEKRIEFDLEYIREWSVWLDIKIVFLTV 454
Cdd:TIGR03022 419 ----YDERVYLDVWYIKNWSLWLDIVILAKTI 446
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
25-454 1.42e-58

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: 199.15  E-value: 1.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   25 DITIMFVGLWVVCRIN---ELPFFYMHLLMALTTLVVF----QMIGGITDFYRSWRGVKISTELLLLLqnwtMSLVFSAG 97
Cdd:TIGR03013   2 ELVVLVLALYLAVLLRffyQIGMFSLLSLVPLAQLVTFalvvIISAIALGLYNVDLREDFRGIIARLA----ISLLVSFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   98 LMAF----NPDFESPFRVYLAWYLLTGAGMVMCRSAIRFgagWLRNRGYNtRRVAIAGAQPVGQQLADSFRNEPWLGFEV 173
Cdd:TIGR03013  78 ALSFifyfYPEFYLGRGLLALAIVLAGSLVLLSRLFFLK---ILGLQGLK-RRILVLGTGPRAREIARLRRSSDRRGHEI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  174 VGIYHDP-EPGGVPT-GWAGNLEQLVEDARTGKIHNVYIAMSmseEAQMKKLVRELSDTTCSVMLIPDVFTFNILHSRLD 251
Cdd:TIGR03013 154 VGFVPLPdEPAYVPSeHVIENGDGLVEYVLRHRIDEIVIALD---ERRGSLPVDELLECKLSGIEVVDAPSFFERETGKI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  252 DVNGV-PVVPLYDTPL--SGINRVLKRLEDIVLASLILLLISPVLCCIAVAVKLSSPGPIIFRQTRYGMDGKPIMVWKFR 328
Cdd:TIGR03013 231 AIDLIyPSWLIFSNGFrnSSLRRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  329 SMRVMENDKVVKQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLRHKVKPGI 408
Cdd:TIGR03013 311 SMRADAEKNGAVWAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGI 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 490521324  409 TGWAQINGWRG--ETDTLEKMekriEFDLEYIREWSVWLDIKIVFLTV 454
Cdd:TIGR03013 391 TGWAQIKYPYGasVADAKEKL----RYDLYYIKNMSLLLDLIILIQTF 434
CoA_binding_3 pfam13727
CoA-binding domain;
65-238 1.87e-46

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 158.58  E-value: 1.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324   65 ITDFYRSWRGVKISTELLLLLQNWTMSLVFSAGLMAFNPDFESpfRVYLAWYLLTGAGMVMCRSAIRF--GAGWLRNRGY 142
Cdd:pfam13727   2 AFGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIFS--RLWLAYWAVSGIALLILSRLLLRavLRRYRRHGRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324  143 NTRRVAIAGAQPVGQQLadsfRNEPWLGFEVVGIYHDPEPGGVPTG----WAGNLEQLVEDARTGKIHNVYIAMSMSEEA 218
Cdd:pfam13727  80 NRRVVAVGGGLELARQI----RANPWLGFRVVGVFDDRDDDRVPEVagvpVLGNLADLVEYVRETRVDEVYLALPLSAEA 155
                         170       180
                  ....*....|....*....|
gi 490521324  219 QMKKLVRELSDTTCSVMLIP 238
Cdd:pfam13727 156 RILRLVKELRDDPVNIRLIP 175
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
137-454 4.22e-40

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 150.16  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 137 LRNR-GYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIYH----DPEPGGVPTGWAGNLeqLVEDARTGKIHNVyIA 211
Cdd:PRK15204 138 LLNKlGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDtdasDAEINMLPVIKDTEI--IWDLNRTGDVHYI-LA 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 212 MSMSEEAQMKKLVRELSDTTC-SVMLIPDVFTfnilhsrlddvngvpvVPLYDTPLSGI------------------NRV 272
Cdd:PRK15204 215 YEYTELEKTHFWLRELSKHHCrSVTVVPSFRG----------------LPLYNTDMSFIfshevmllriqnnlakrsSRF 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 273 LKRLEDIVLASLILLLISPVLCCIAVAVKLSSpGPIIFRQTRYGMDGKPIMVWKFRSMrVMENDKVVKQ----------- 341
Cdd:PRK15204 279 LKRTFDIVCSIMILIIASPLMIYLWYKVTRDG-GPAIYGHQRVGRHGKLFPCYKFRSM-VMNSQEVLKEllandpiarae 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 342 -----ATQNDPRVTKVGNFLRRTSLDELPQFINVLTGEMSIVGPRPHAVAHNEQYRALIQGYMLrhkVKPGITGWAQING 416
Cdd:PRK15204 357 wekdfKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG 433
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490521324 417 wRGETDtlekMEKRIEFDLEYIREWSVWLDIKIVFLTV 454
Cdd:PRK15204 434 -RNDVD----YDTRVYFDSWYVKNWTLWNDIAILFKTA 466
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
124-239 7.10e-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: 98.84  E-value: 7.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521324 124 VMCRSAIRFGAGWLRNRGYNTRRVAIAGAQPVGQQLADSFRNEPWLGFEVVGIY------HDPEPGGVPtgWAGNLEQLV 197
Cdd:COG1086    1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVdddpdkRGRRIEGVP--VLGTLDDLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490521324 198 EDARTGKIHNVYIAMSMSEEAQMKKLVRELSDTTCSVMLIPD 239
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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