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Conserved domains on  [gi|521350320|gb|AGQ01504|]
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lipopolysaccharide synthesis sugar transferase [Alteromonas mediterranea UM4b]

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. ...
38-484 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: 607.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   38 LIDLSLVTL-LYYSCAAYFESTIDPTS---LILLFVNVICFQISAEGVELYRSWRGHRTPEMLRAAAITWALSILGTLTI 113
Cdd:TIGR03023   1 LLDLLLIALaLLLAYLLRFGSRGPPDIesyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  114 GYFFVQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMF 193
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  194 DDR-DAERLPHDMQnsVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNLLNARWQT 272
Cdd:TIGR03023 161 DDRpDARTSVRGVP--VLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  273 VGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTT 352
Cdd:TIGR03023 239 IGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  353 QDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVKPGITGWA 432
Cdd:TIGR03023 319 HAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 521350320  433 QVNGLRGETETVNKMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
38-484 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: 607.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   38 LIDLSLVTL-LYYSCAAYFESTIDPTS---LILLFVNVICFQISAEGVELYRSWRGHRTPEMLRAAAITWALSILGTLTI 113
Cdd:TIGR03023   1 LLDLLLIALaLLLAYLLRFGSRGPPDIesyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  114 GYFFVQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMF 193
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  194 DDR-DAERLPHDMQnsVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNLLNARWQT 272
Cdd:TIGR03023 161 DDRpDARTSVRGVP--VLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  273 VGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTT 352
Cdd:TIGR03023 239 IGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  353 QDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVKPGITGWA 432
Cdd:TIGR03023 319 HAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 521350320  433 QVNGLRGETETVNKMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
28-484 6.29e-171

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 489.23  E-value: 6.29e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  28 NKSGFSTLYRLIDLSLVTL-LYYSCAAYFESTIDPTSLILLFVNVIcFQISAEGVELYRSWRGHRTPEMLRAAAITWALS 106
Cdd:PRK10124  12 NASLISMVQRFSDITIMFAgLWLVCEVSGLSFLYMHLLVALITLVV-FQMLGGITDFYRSWRGVKASTELALLLQNWTLS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 107 ILgtLTIGYF-FVQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHL 185
Cdd:PRK10124  91 LI--FSAGLVaFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 186 GIRFNGMFDDRdaerLPHDMQNSVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNL 265
Cdd:PRK10124 169 GFEVVGVYHDP----KPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNI 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 266 LNARWQTVGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVY 345
Cdd:PRK10124 245 LHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVW 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 346 KFRSMTTQDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVK 425
Cdd:PRK10124 325 KFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVK 404
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521350320 426 PGITGWAQVNGLRGETETVNKMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:PRK10124 405 PGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
147-483 2.00e-110

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 329.77  E-value: 2.00e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 147 RKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMFDDRDAERLPHDMQNSVLGNIEQAIEMAKRNEVD 226
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 227 YIYIALPMSAENRIRSILEQCSDTTANvyvvpnffmYNLLNARWQTVGNVQALSVYDTPFQGASDVLKRFEDIVLSSLIL 306
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 307 MMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTTQ-DNGAVVKQATKNDARLTKIGGFLRRTSLDELP 385
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 386 QFINVLQGRMSIVGPRPHAVAHNEQYRKiiTGYMLRHKVKPGITGWAQVNGLRGETetvnkMVQRVEYDLDYIHRWSVWF 465
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 521350320 466 DIKIVFMTVFNGFINKNA 483
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
294-478 8.16e-94

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: 281.94  E-value: 8.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  294 KRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTTQDNGAVVKQATKNDARLTKIG 373
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  374 GFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHneQYRKIITGYMLRHKVKPGITGWAQVNGLRGETetvnKMVQRVEY 453
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSEL----SFEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 521350320  454 DLDYIHRWSVWFDIKIVFMTVFNGF 478
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. ...
38-484 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: 607.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   38 LIDLSLVTL-LYYSCAAYFESTIDPTS---LILLFVNVICFQISAEGVELYRSWRGHRTPEMLRAAAITWALSILGTLTI 113
Cdd:TIGR03023   1 LLDLLLIALaLLLAYLLRFGSRGPPDIesyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  114 GYFFVQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMF 193
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  194 DDR-DAERLPHDMQnsVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNLLNARWQT 272
Cdd:TIGR03023 161 DDRpDARTSVRGVP--VLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  273 VGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTT 352
Cdd:TIGR03023 239 IGGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  353 QDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVKPGITGWA 432
Cdd:TIGR03023 319 HAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 521350320  433 QVNGLRGETETVNKMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
38-484 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: 521.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   38 LIDLSLVTLLYYSCAAYFESTIDPTS-----LILLFVNVICFQISAEGveLYRSWRGHRTPEMLRAAAITWALSILGTLT 112
Cdd:TIGR03025   1 LADLLALVLAFLLAFLLLGLGLLPPPdfyslLLLLLLLLFLILFALSG--LYRSWRGRSLLEELARVLLAWLVAFLLLLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  113 IGYFFvQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGM 192
Cdd:TIGR03025  79 LAFLF-KSFDFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  193 FDDRDAERLPHDMQNsVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNLLNARWQT 272
Cdd:TIGR03025 158 VDDRPSDRVEVAGLP-VLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  273 VGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTT 352
Cdd:TIGR03025 237 LGGVPLLSLSNFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  353 -QDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVKPGITGW 431
Cdd:TIGR03025 317 dAEEGGGPVQATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGW 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 521350320  432 AQVNGlRGETETvnkMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:TIGR03025 397 AQVSG-RGETST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
28-484 6.29e-171

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 489.23  E-value: 6.29e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  28 NKSGFSTLYRLIDLSLVTL-LYYSCAAYFESTIDPTSLILLFVNVIcFQISAEGVELYRSWRGHRTPEMLRAAAITWALS 106
Cdd:PRK10124  12 NASLISMVQRFSDITIMFAgLWLVCEVSGLSFLYMHLLVALITLVV-FQMLGGITDFYRSWRGVKASTELALLLQNWTLS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 107 ILgtLTIGYF-FVQNINTPPFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHL 185
Cdd:PRK10124  91 LI--FSAGLVaFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 186 GIRFNGMFDDRdaerLPHDMQNSVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNFFMYNL 265
Cdd:PRK10124 169 GFEVVGVYHDP----KPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNI 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 266 LNARWQTVGNVQALSVYDTPFQGASDVLKRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVY 345
Cdd:PRK10124 245 LHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVW 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 346 KFRSMTTQDNGAVVKQATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVK 425
Cdd:PRK10124 325 KFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVK 404
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521350320 426 PGITGWAQVNGLRGETETVNKMVQRVEYDLDYIHRWSVWFDIKIVFMTVFNGFINKNAY 484
Cdd:PRK10124 405 PGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
147-483 2.00e-110

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 329.77  E-value: 2.00e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 147 RKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMFDDRDAERLPHDMQNSVLGNIEQAIEMAKRNEVD 226
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 227 YIYIALPMSAENRIRSILEQCSDTTANvyvvpnffmYNLLNARWQTVGNVQALSVYDTPFQGASDVLKRFEDIVLSSLIL 306
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 307 MMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTTQ-DNGAVVKQATKNDARLTKIGGFLRRTSLDELP 385
Cdd:COG2148  152 ILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 386 QFINVLQGRMSIVGPRPHAVAHNEQYRKiiTGYMLRHKVKPGITGWAQVNGLRGETetvnkMVQRVEYDLDYIHRWSVWF 465
Cdd:COG2148  232 QLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWL 304
                        330
                 ....*....|....*...
gi 521350320 466 DIKIVFMTVFNGFINKNA 483
Cdd:COG2148  305 DLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
294-478 8.16e-94

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: 281.94  E-value: 8.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  294 KRFEDIVLSSLILMMISIPMLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMTTQDNGAVVKQATKNDARLTKIG 373
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  374 GFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHneQYRKIITGYMLRHKVKPGITGWAQVNGLRGETetvnKMVQRVEY 453
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSEL----SFEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 521350320  454 DLDYIHRWSVWFDIKIVFMTVFNGF 478
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
61-474 9.19e-59

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: 199.92  E-value: 9.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   61 PTSLILLFVNVIcfQISAEGVELYRSWRGHRTPEMLRAAAITWALSILGTLTIGYF---FVQNINTPPFIILAWFAtsfv 137
Cdd:TIGR03013  32 PLAQLVTFALVV--IISAIALGLYNVDLREDFRGIIARLAISLLVSFLALSFIFYFypeFYLGRGLLALAIVLAGS---- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  138 GLIAWRFVMRKFLFRirksGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMFDDRDAE-RLPHDmqnSVLGNIEQA 216
Cdd:TIGR03013 106 LVLLSRLFFLKILGL----QGLKRRILVLGTGPRAREIARLRRSSDRRGHEIVGFVPLPDEPaYVPSE---HVIENGDGL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  217 IEMAKRNEVDYIYIALpmsAENR----IRSILEqCSDTTANVYVVPNFF-------MYNLLNARWQtvgnvqalsVYDTP 285
Cdd:TIGR03013 179 VEYVLRHRIDEIVIAL---DERRgslpVDELLE-CKLSGIEVVDAPSFFeretgkiAIDLIYPSWL---------IFSNG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  286 FQGAS--DVLKRFEDIVlSSLILMMISIP-MLCIAAAVKLTSKGPVIFKQKRYGLDGKQITVYKFRSMT--TQDNGAVvk 360
Cdd:TIGR03013 246 FRNSSlrRITKRSFDVV-ASLILLILTLPvMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRadAEKNGAV-- 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  361 QATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYMLRHKVKPGITGWAQVNGLRGE 440
Cdd:TIGR03013 323 WAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGA 402
                         410       420       430
                  ....*....|....*....|....*....|....
gi 521350320  441 TETVNKmvQRVEYDLDYIHRWSVWFDIKIVFMTV 474
Cdd:TIGR03013 403 SVADAK--EKLRYDLYYIKNMSLLLDLIILIQTF 434
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
131-474 2.11e-39

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 148.61  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 131 WFATSFVGLIAWRFVMRKF-LFR------IRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMFD----DRDAE 199
Cdd:PRK15204 110 WQFSRYVWVFCWTFALILVpFFRaltkhlLNKLGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDtdasDAEIN 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 200 RLPhdmqnsVLGNIEQAIEMAKRNEVDYIyIALPMSAENRIRSILEQCSDTTA-NVYVVPNFFMYNLLNARWQTV--GNV 276
Cdd:PRK15204 190 MLP------VIKDTEIIWDLNRTGDVHYI-LAYEYTELEKTHFWLRELSKHHCrSVTVVPSFRGLPLYNTDMSFIfsHEV 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 277 QALSVYDTPFQGASDVLKRFEDIVLSSLILMmISIPMLcIAAAVKLTSKG-PVIFKQKRYGLDGKQITVYKFRSMTTQ-- 353
Cdd:PRK15204 263 MLLRIQNNLAKRSSRFLKRTFDIVCSIMILI-IASPLM-IYLWYKVTRDGgPAIYGHQRVGRHGKLFPCYKFRSMVMNsq 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 354 -------DNGAVVKQ------ATKNDARLTKIGGFLRRTSLDELPQFINVLQGRMSIVGPRPHAVAHNEQYRKIITGYML 420
Cdd:PRK15204 341 evlkellANDPIARAewekdfKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM 420
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521350320 421 rhkVKPGITGWAQVNGlRGETETVNkmvqRVEYDLDYIHRWSVWFDIKIVFMTV 474
Cdd:PRK15204 421 ---AKPGMTGLWQVSG-RNDVDYDT----RVYFDSWYVKNWTLWNDIAILFKTA 466
CoA_binding_3 pfam13727
CoA-binding domain;
83-258 2.38e-37

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 135.09  E-value: 2.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320   83 LYRSWRGHRTPEMLRAAAITWALSILGTLTIGYFFVQNINTppFIILAWFATSFVGLIAWRFVMRKFLFRIRKSGMNSRR 162
Cdd:pfam13727   5 VYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIFSR--LWLAYWAVSGIALLILSRLLLRAVLRRYRRHGRNNRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320  163 sivIGATHLGANVALQIQQNEHLGIRFNGMFDDRDAERLPHDMQNSVLGNIEQAIEMAKRNEVDYIYIALPMSAENRIRS 242
Cdd:pfam13727  83 ---VVAVGGGLELARQIRANPWLGFRVVGVFDDRDDDRVPEVAGVPVLGNLADLVEYVRETRVDEVYLALPLSAEARILR 159
                         170
                  ....*....|....*.
gi 521350320  243 ILEQCSDTTANVYVVP 258
Cdd:pfam13727 160 LVKELRDDPVNIRLIP 175
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
140-260 2.83e-30

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: 113.87  E-value: 2.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521350320 140 IAWRFVMRKFLFRIRKSGMNSRRSIVIGATHLGANVALQIQQNEHLGIRFNGMFDDRDAERLPHDMQNSVLGNIEQAIEM 219
Cdd:COG1086    1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPDKRGRRIEGVPVLGTLDDLPEL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 521350320 220 AKRNEVDYIYIALPMSAENRIRSILEQCSDTTANVYVVPNF 260
Cdd:COG1086   81 VRRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPDL 121
 
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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