WECF_YERPA
ID WECF_YERPA Reviewed; 361 AA.
AC Q1CBP2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01002};
DE EC=2.4.1.325 {ECO:0000255|HAMAP-Rule:MF_01002};
DE AltName: Full=4-alpha-L-fucosyltransferase {ECO:0000255|HAMAP-Rule:MF_01002};
DE AltName: Full=TDP-Fuc4NAc:lipid II Fuc4NAc transferase {ECO:0000255|HAMAP-Rule:MF_01002};
DE Short=Fuc4NAc transferase {ECO:0000255|HAMAP-Rule:MF_01002};
GN Name=wecF {ECO:0000255|HAMAP-Rule:MF_01002};
GN Synonyms=rffT {ECO:0000255|HAMAP-Rule:MF_01002};
GN OrderedLocusNames=YPA_0161;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
CC -!- FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc
CC (Lipid III), the third lipid-linked intermediate involved in ECA
CC synthesis. {ECO:0000255|HAMAP-Rule:MF_01002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-di-trans,octa-cis-
CC undecaprenyl diphosphate + dTDP-4-acetamido-4,6-dideoxy-alpha-D-
CC galactose = alpha-D-FucNAc4-(1->4)-beta-D-ManNAcA-(1->4)-D-GlcNAc-
CC undecaprenyl diphosphate + dTDP + H(+); Xref=Rhea:RHEA:28759,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58369, ChEBI:CHEBI:61495,
CC ChEBI:CHEBI:61496, ChEBI:CHEBI:68493; EC=2.4.1.325;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01002};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01002}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01002}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01002}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 56 family.
CC {ECO:0000255|HAMAP-Rule:MF_01002}.
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DR EMBL; CP000308; ABG12130.1; -; Genomic_DNA.
DR RefSeq; WP_002211979.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1CBP2; -.
DR SMR; Q1CBP2; -.
DR CAZy; GT56; Glycosyltransferase Family 56.
DR EnsemblBacteria; ABG12130; ABG12130; YPA_0161.
DR GeneID; 57974846; -.
DR KEGG; ypa:YPA_0161; -.
DR OMA; VIVPMGY; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001971; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102031; F:4-acetamido-4,6-dideoxy-D-galactose transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008417; F:fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0036065; P:fucosylation; IEA:InterPro.
DR HAMAP; MF_01002; WecF_RffT; 1.
DR InterPro; IPR009993; WecF.
DR Pfam; PF07429; Glyco_transf_56; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Transferase.
FT CHAIN 1..361
FT /note="TDP-N-acetylfucosamine:lipid II N-
FT acetylfucosaminyltransferase"
FT /id="PRO_1000062752"
SQ SEQUENCE 361 AA; 41071 MW; FDA273D7B5A2FD90 CRC64;
MITLTHVLGS DIPHHNLTVL RFFNDVLAKC LPVEQVRHFM VAAKETAPFS SFPQLDINTY
SDKKALAEAV IARAQADRSA RFFWHGQFNV TLWLALLSGK IKPGQVYWHV WGADLYEDAK
SLKFRLFYLL RRIAQGRVGH VFATRGDLIH YQQRHPRVPA SLLYFPTRMD PALTAINIDK
PLAGPMTILV GNSGDTTNRH IEALKAIHQQ FGPDVRVIIP MGYPANNEAY IEQVRQAGLA
LFSQDNLRIL TEQIPFDDYL NILRECDLGY FIFNRQQGIG TLCLLTQFGV PFVLSRKNPF
WQDLAEQHIP VFFYGDTLDE PMIREAQRQL AGLDKQAIAF FNPNYIEGWK QALALAAGEH
P