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WECA_SALTI
ID   WECA_SALTI              Reviewed;         367 AA.
AC   Q8Z386;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 126.
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=STY3637, t3379;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD09398.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70903.1; -; Genomic_DNA.
DR   RefSeq; NP_457829.1; NC_003198.1.
DR   RefSeq; WP_000771938.1; NZ_UCTX01000015.1.
DR   AlphaFoldDB; Q8Z386; -.
DR   SMR; Q8Z386; -.
DR   STRING; 220341.16504516; -.
DR   EnsemblBacteria; AAO70903; AAO70903; t3379.
DR   KEGG; stt:t3379; -.
DR   KEGG; sty:STY3637; -.
DR   PATRIC; fig|220341.7.peg.3706; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_1_0_6; -.
DR   OMA; MCLGFLP; -.
DR   UniPathway; UPA00281; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000108944"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT   TRANSMEM        45..65
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        129..149
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        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
SQ   SEQUENCE   367 AA;  41086 MW;  28DA31CB1AE2D930 CRC64;
     MKLLTALSEL ISIFLFTTIF IFLARKVAIK IGLVDKPNFR KRHQGVIPLV GGISVFAGIC
     FMFGLSDYYI PHLSLYLICA GVLVFVGAMD DRFDISVKIR AVVQAVIAVV MMVIAKLHLG
     SLGYIFGPWE LVLGPFGYFL TLFAVWAAIN AFNMVDGIDG LLGGLSSVSF AAMGLILWFD
     GQTSLAMWCF AMIAAILPYI MLNLGILGRR YKVFMGDAGS TLIGFTVIWL LLETTQGKTH
     SISPVTALWI IAIPLMDMVA IMYRRLRKGM SPFSPDRQHI HHLVMRAGFT SRQAFVLITL
     AAAILAGVGV TAEYSHFVPE WVMLVLFLLA FFLYGYCIKR AWKVARFIKR VKRRLRRQRK
     NRPNLTK
 
 
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