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WECA_ECOL6
ID   WECA_ECOL6              Reviewed;         367 AA.
AC   P0AC79; P24235; P76751; Q9F8C8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
DE            EC=2.7.8.33 {ECO:0000255|HAMAP-Rule:MF_02030};
DE   AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
DE   AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
GN   Name=wecA {ECO:0000255|HAMAP-Rule:MF_02030}; Synonyms=rfe;
GN   OrderedLocusNames=c4704;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from
CC       UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC       yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55).
CC       {ECO:0000255|HAMAP-Rule:MF_02030}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC         D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC         undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC         ChEBI:CHEBI:62959; EC=2.7.8.33; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02030};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02030};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC       antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02030}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02030}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02030}.
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DR   EMBL; AE014075; AAN83137.1; -; Genomic_DNA.
DR   RefSeq; WP_001050960.1; NC_004431.1.
DR   AlphaFoldDB; P0AC79; -.
DR   SMR; P0AC79; -.
DR   STRING; 199310.c4704; -.
DR   EnsemblBacteria; AAN83137; AAN83137; c4704.
DR   GeneID; 66672313; -.
DR   KEGG; ecc:c4704; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_1_0_6; -.
DR   OMA; MCLGFLP; -.
DR   BioCyc; ECOL199310:C4704-MON; -.
DR   UniPathway; UPA00281; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; ISS:UniProtKB.
DR   GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044038; P:cell wall macromolecule biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; ISS:UniProtKB.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR   InterPro; IPR012750; ECA_WecA-rel.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   PANTHER; PTHR22926; PTHR22926; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   TIGRFAMs; TIGR02380; ECA_wecA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Glycosyltransferase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Manganese; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-
FT                   phosphate transferase"
FT                   /id="PRO_0000108943"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
SQ   SEQUENCE   367 AA;  40957 MW;  6EB11CC80C6B9CC8 CRC64;
     MNLLTVSTDL ISIFLFTTLF LFFARKVAKK VGLVDKPNFR KRHQGLIPLV GGISVYAGIC
     FTFGIVDYYI PHASLYLACA GVLVFIGALD DRFDISVKIR ATIQAAVGIV MMVFGKLYLS
     SLGYIFGSWE MVLGPFGYFL TLFAVWAAIN AFNMVDGIDG LLGGLSCVSF AAIGMILWFD
     GQTSLAIWCF AMIAAILPYI MLNLGILGRR YKVFMGDAGS TLIGFTVIWI LLETTQGKTH
     PISPVTALWI IAIPLMDMVA IMYRRLRKGM SPFSPDRQHI HHLIMRAGFT SRQAFVLITL
     AAALLASIGV LAEYSHFVPE WVMLVLFLLA FFLYGYCIKR AWKVARFIKR VKRRLRRNRG
     GSPNLTK
 
 
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