WECF_ECO81
ID WECF_ECO81 Reviewed; 359 AA.
AC B7MR14;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=ECED1_4478;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10597.2; -; Genomic_DNA.
DR RefSeq; WP_000217277.1; NC_011745.1.
DR AlphaFoldDB; B7MR14; -.
DR SMR; B7MR14; -.
DR CAZy; GT56; Glycosyltransferase Family 56.
DR EnsemblBacteria; CAR10597; CAR10597; ECED1_4478.
DR KEGG; ecq:ECED1_4478; -.
DR HOGENOM; CLU_066584_0_0_6; -.
DR OMA; VIVPMGY; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000748; 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..359
FT /note="TDP-N-acetylfucosamine:lipid II N-
FT acetylfucosaminyltransferase"
FT /id="PRO_1000148785"
SQ SEQUENCE 359 AA; 40529 MW; B1FD252D7E7CAB70 CRC64;
MTVLIHVLGS DIPHHNRTVL RFFNDALAAT SGHAREFMVA GKDDGLSDSC PALSVQFFPG
KKSLAEAVIA KAKANRQQRF FFHGQFNPKL WLALLSGGIK PSQFFWHIWG ADLYELSSGL
RYKLFYPLRR LAQKRVGCVF ATRGDLSFFA KTHPKVRGEL LYFPTRMDPS LNTMANDRQR
EGKMTILVGN SGDRSNEHIA ALRAVHQQFG DTVKVVVPMG YPPNNEAYIE EVRQAGLELF
SEENLQVLSE KLEFDAYLTL LRQCDLGYFI FARQQGIGTL CLLIQAGIPC VLNRENPFWQ
DMTEQHLPVL FTTDDLNEDI VREAQRQLAS VDKNTIAFFS PNYLQGWQRA LAIATGEVA