ID   WECF_SHIDS              Reviewed;         359 AA.
AC   Q329X1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SDY_3955;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000034; ABB63884.1; -; Genomic_DNA.
DR   RefSeq; WP_000217226.1; NC_007606.1.
DR   RefSeq; YP_405375.1; NC_007606.1.
DR   AlphaFoldDB; Q329X1; -.
DR   SMR; Q329X1; -.
DR   STRING; 300267.SDY_3955; -.
DR   CAZy; GT56; Glycosyltransferase Family 56.
DR   EnsemblBacteria; ABB63884; ABB63884; SDY_3955.
DR   KEGG; sdy:SDY_3955; -.
DR   PATRIC; fig|300267.13.peg.4666; -.
DR   HOGENOM; CLU_066584_0_0_6; -.
DR   OMA; VIVPMGY; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000002716; 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   Reference proteome; Transferase.
FT   CHAIN           1..359
FT                   /note="TDP-N-acetylfucosamine:lipid II N-
FT                   acetylfucosaminyltransferase"
FT                   /id="PRO_1000062747"
SQ   SEQUENCE   359 AA;  40553 MW;  9AA31A4CB1B27BBE CRC64;
     MTVLIHVLGS DIPHHNRTVL RFFNDALAAT SEHAREFMVV GKDDGLSDSC PALSVQFFPG
     KKSLAEAVIA KAKANRQQRF FFHGQFNPKL WLALLSGGIK SRQFFWHIWG ADLYELSSGL
     IYKLFYPLRR LAQKRVGCVF ATRGDLSFFA KTHPKVRGEL LYFPTRMDPS LNTLANDRQR
     EGKMTILVGN SGDRSNEHVA ALRAVHQQFG DTVKVVVPMG YPPNNEAYIE EVRQAGLELF
     SEENLQVLSE KLEFDAYLAL LRQCDLGYFI FARQQGIGTL CLLIQAGIPC VLNRENPFWQ
     DMTEQHLPVL FTTDDLNEDI VREAQRQLAS VDKNTIAFFS PNYLQGWQRA LAIAAGEVA