ID   WECF_SHIB3              Reviewed;         359 AA.
AC   B2TU00;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=SbBS512_E4128;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD08940.1; -; Genomic_DNA.
DR   RefSeq; WP_000217241.1; NC_010658.1.
DR   AlphaFoldDB; B2TU00; -.
DR   SMR; B2TU00; -.
DR   STRING; 344609.SbBS512_E4128; -.
DR   CAZy; GT56; Glycosyltransferase Family 56.
DR   EnsemblBacteria; ACD08940; ACD08940; SbBS512_E4128.
DR   KEGG; sbc:SbBS512_E4128; -.
DR   HOGENOM; CLU_066584_0_0_6; -.
DR   OMA; VIVPMGY; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001030; 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_1000134611"
SQ   SEQUENCE   359 AA;  40542 MW;  31CD6A93A72AFAFB CRC64;
     MTVLIHVLGS DIPHHNRTVL RFFNDALAAT SEHAREFMVV GKDDGLSDSC PALSVQFFPG
     KKSLAEAVIA KAKANRQQRF FFHGQFNPTL WLALLSGGIK PSQFFWHIWG ADLYELSSGL
     RYKLFYPLRR LAQKRVGCVF ATRGDLSFFA KTHPKVRGEL LYFPTRMDPS LNTMANDRQR
     EGKMTILVGN SGDRSNDHIA ALRAVHQQFG DTVKVVVPMG YPPNNEAYIE EVRQAGLELF
     SEENLQILSE KLEFDAYLAL LRQCDLGYFI FARQQGIGTL CLLIQAGIPC VLNRENPFWQ
     DMTEQHLPVL FTTDDLNEDI VREAQRQLAS VDKNTIAFFS PNYLQGWQRA LAIAAGEVA