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Conserved domains on  [gi|617074575|gb|KAI59892|]
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hypothetical protein W809_00391 [Staphylococcus aureus VET1950S]

Protein Classification

sugar transferase( domain architecture ID 10005412)

sugar transferase catalyzes the transfer of a sugar from a donor such as UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate

EC:  2.-.-.-
Gene Ontology:  GO:0016780|GO:0000271|GO:0005886
PubMed:  29769739
SCOP:  4007826

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
1-183 7.67e-91

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


:

Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 268.14  E-value: 7.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKIDTPNV--ATDLMDSTSYITK 78
Cdd:COG2148  138 LKRLFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLlgAVFKLKNDPRITR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  79 TGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTKANVHTIRPGVTGLAQVMGRDDITDDQKVAYDHYYL 158
Cdd:COG2148  218 VGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEEEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYI 297
                        170       180
                 ....*....|....*....|....*
gi 617074575 159 THQSMMLDMYIIYKTIKNIVTSEGV 183
Cdd:COG2148  298 ENWSLWLDLKILLKTVLVVLKGKGA 322
 
Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
1-183 7.67e-91

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 268.14  E-value: 7.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKIDTPNV--ATDLMDSTSYITK 78
Cdd:COG2148  138 LKRLFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLlgAVFKLKNDPRITR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  79 TGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTKANVHTIRPGVTGLAQVMGRDDITDDQKVAYDHYYL 158
Cdd:COG2148  218 VGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEEEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYI 297
                        170       180
                 ....*....|....*....|....*
gi 617074575 159 THQSMMLDMYIIYKTIKNIVTSEGV 183
Cdd:COG2148  298 ENWSLWLDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
2-179 7.87e-87

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: 252.67  E-value: 7.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575    2 KRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKIDTPNVATDL-MDSTSYITKTG 80
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFkLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   81 KVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTKANVHTIRPGVTGLAQVM-GRDDITDDQKVAYDHYYLT 159
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEFEYELYERDQRRRLSVKPGITGLAQVNgGRSELSFEEKLELDLYYIE 160
                         170       180
                  ....*....|....*....|
gi 617074575  160 HQSMMLDMYIIYKTIKNIVT 179
Cdd:pfam02397 161 NWSLWLDLKILLKTVKVVLK 180
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
1-182 5.55e-76

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: 234.02  E-value: 5.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575    1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKID--TPNVATDLMDSTSYITK 78
Cdd:TIGR03025 257 LKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaeEGGGPVQATKNDPRITR 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   79 TGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTK--ANVHTIRPGVTGLAQVMGRDDITD-DQKVAYDH 155
Cdd:TIGR03025 337 VGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPgyMLRHKVKPGITGWAQVSGRGETSTmEERVEYDL 416
                         170       180
                  ....*....|....*....|....*..
gi 617074575  156 YYLTHQSMMLDMYIIYKTIKNIVTSEG 182
Cdd:TIGR03025 417 YYIENWSLWLDLKILLKTVKVVLTGKG 443
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-174 1.43e-40

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 142.55  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKI-DTPNVATDLMDSTSYITKT 79
Cdd:PRK10124 272 LKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVmENDKVVTQATQNDPRVTKV 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  80 GKVIRKTSIDELPQLLNVLKGEMSIVGPRP---ALYNQY-ELIEKRTKAnvHTIRPGVTGLAQVMGRDDITD-----DQK 150
Cdd:PRK10124 352 GNFLRRTSLDELPQFINVLTGGMSIVGPRPhavAHNEQYrQLIEGYMLR--HKVKPGITGWAQINGWRGETDtlekmEKR 429
                        170       180
                 ....*....|....*....|....
gi 617074575 151 VAYDHYYLTHQSMMLDMYIIYKTI 174
Cdd:PRK10124 430 VEFDLEYIREWSVWFDIKIVFLTV 453
 
Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
1-183 7.67e-91

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 268.14  E-value: 7.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKIDTPNV--ATDLMDSTSYITK 78
Cdd:COG2148  138 LKRLFDIVLALLGLILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLlgAVFKLKNDPRITR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  79 TGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTKANVHTIRPGVTGLAQVMGRDDITDDQKVAYDHYYL 158
Cdd:COG2148  218 VGRFLRKTSLDELPQLWNVLKGDMSLVGPRPELPEEVELYEEEEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYI 297
                        170       180
                 ....*....|....*....|....*
gi 617074575 159 THQSMMLDMYIIYKTIKNIVTSEGV 183
Cdd:COG2148  298 ENWSLWLDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
2-179 7.87e-87

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: 252.67  E-value: 7.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575    2 KRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKIDTPNVATDL-MDSTSYITKTG 80
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFkLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   81 KVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTKANVHTIRPGVTGLAQVM-GRDDITDDQKVAYDHYYLT 159
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEFEYELYERDQRRRLSVKPGITGLAQVNgGRSELSFEEKLELDLYYIE 160
                         170       180
                  ....*....|....*....|
gi 617074575  160 HQSMMLDMYIIYKTIKNIVT 179
Cdd:pfam02397 161 NWSLWLDLKILLKTVKVVLK 180
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
1-182 5.55e-76

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: 234.02  E-value: 5.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575    1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKID--TPNVATDLMDSTSYITK 78
Cdd:TIGR03025 257 LKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaeEGGGPVQATKNDPRITR 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   79 TGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYELIEKRTK--ANVHTIRPGVTGLAQVMGRDDITD-DQKVAYDH 155
Cdd:TIGR03025 337 VGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPgyMLRHKVKPGITGWAQVSGRGETSTmEERVEYDL 416
                         170       180
                  ....*....|....*....|....*..
gi 617074575  156 YYLTHQSMMLDMYIIYKTIKNIVTSEG 182
Cdd:TIGR03025 417 YYIENWSLWLDLKILLKTVKVVLTGKG 443
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
1-174 1.12e-69

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: 218.22  E-value: 1.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575    1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKI----DTPNVAT--DlmdstS 74
Cdd:TIGR03023 259 IKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVhaegDGVTQATrnD-----P 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   75 YITKTGKVIRKTSIDELPQLLNVLKGEMSIVGPRP-ALY--NQY-ELIEK---RtkanvHTIRPGVTGLAQVMG-RDDIT 146
Cdd:TIGR03023 334 RVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPhAVAhnEQYrKLIPGymlR-----HKVKPGITGWAQVNGlRGETD 408
                         170       180       190
                  ....*....|....*....|....*....|..
gi 617074575  147 DDQK----VAYDHYYLTHQSMMLDMYIIYKTI 174
Cdd:TIGR03023 409 TLEKmekrVEYDLYYIENWSLWLDLKIILLTV 440
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-174 1.43e-40

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 142.55  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESPGPAIFKQKRPTINNELFNIYKFRSMKI-DTPNVATDLMDSTSYITKT 79
Cdd:PRK10124 272 LKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVmENDKVVTQATQNDPRVTKV 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  80 GKVIRKTSIDELPQLLNVLKGEMSIVGPRP---ALYNQY-ELIEKRTKAnvHTIRPGVTGLAQVMGRDDITD-----DQK 150
Cdd:PRK10124 352 GNFLRRTSLDELPQFINVLTGGMSIVGPRPhavAHNEQYrQLIEGYMLR--HKVKPGITGWAQINGWRGETDtlekmEKR 429
                        170       180
                 ....*....|....*....|....
gi 617074575 151 VAYDHYYLTHQSMMLDMYIIYKTI 174
Cdd:PRK10124 430 VEFDLEYIREWSVWFDIKIVFLTV 453
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
1-184 5.36e-40

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 141.30  E-value: 5.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575   1 MKRLFDVVSSIYGLVVLSPILLITALLIKMESpGPAIFKQKRPTINNELFNIYKFRSMKIDTPNVATDLMDSTSY----- 75
Cdd:PRK15204 279 LKRTFDIVCSIMILIIASPLMIYLWYKVTRDG-GPAIYGHQRVGRHGKLFPCYKFRSMVMNSQEVLKELLANDPIaraew 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 617074575  76 -----------ITKTGKVIRKTSIDELPQLLNVLKGEMSIVGPRPALYNQYEliekRTKANVH---TIRPGVTGLAQVMG 141
Cdd:PRK15204 358 ekdfklkndprITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELE----RYCDDVDyylMAKPGMTGLWQVSG 433
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 617074575 142 RDDITDDQKVAYDHYYLTHQSMMLDMYIIYKTIKNIVTSEGVH 184
Cdd:PRK15204 434 RNDVDYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDGAY 476
 
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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