WECF_SALHS
ID WECF_SALHS Reviewed; 359 AA.
AC B4TB25;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=SeHA_C4256;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF68716.1; -; Genomic_DNA.
DR RefSeq; WP_000217183.1; NC_011083.1.
DR AlphaFoldDB; B4TB25; -.
DR CAZy; GT56; Glycosyltransferase Family 56.
DR KEGG; seh:SeHA_C4256; -.
DR HOGENOM; CLU_066584_0_0_6; -.
DR OMA; VIVPMGY; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001866; 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_1000134607"
SQ SEQUENCE 359 AA; 40589 MW; C10BB0FB27720B22 CRC64;
MTVLIHVLGS DIPHHNHTVL RFFNDTLAAT SEHAREFMVA GEDNGFTESC PALSLRFYGS
KKALAQAVIA KAKANRRQRF FFHGQFNTSL WLALLSGGIK PAQFYWHIWG ADLYEVSHGL
KFRLFYPLRR IAQGRVGCVF ATRGDLSYFA RQHPDVRGEL LYFPTRMDPS LNAMAKERQR
AGKLTILVGN SGDRSNQHIA ALRAVYQQFG DTVNVVVPMG YPANNQAYID EVRQAGLALF
SDENLQILSE KMEFDAYLAL LRQCDLGYFI FARQQGIGTL CLLIQADIPC VLNRDNPFWQ
DMAEQHLPVL FTTDDLNEQV VREAQRQLAS VDKSGITFFS PNYLQPWHNA LRIAAGEAE
