ID   WECF_ECOUT              Reviewed;         359 AA.
AC   Q1R4E3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-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=UTI89_C4350;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE09771.1; -; Genomic_DNA.
DR   RefSeq; WP_000217276.1; NC_007946.1.
DR   AlphaFoldDB; Q1R4E3; -.
DR   SMR; Q1R4E3; -.
DR   CAZy; GT56; Glycosyltransferase Family 56.
DR   EnsemblBacteria; ABE09771; ABE09771; UTI89_C4350.
DR   KEGG; eci:UTI89_C4350; -.
DR   HOGENOM; CLU_066584_0_0_6; -.
DR   OMA; VIVPMGY; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001952; 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_1000062744"
SQ   SEQUENCE   359 AA;  40499 MW;  B1FD252D620CAB70 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 LAIAAGEVA