WECF_SHIF8
ID WECF_SHIF8 Reviewed; 359 AA.
AC Q0SYY3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-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=SFV_3711;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF05732.1; -; Genomic_DNA.
DR RefSeq; WP_000217247.1; NC_008258.1.
DR AlphaFoldDB; Q0SYY3; -.
DR SMR; Q0SYY3; -.
DR CAZy; GT56; Glycosyltransferase Family 56.
DR EnsemblBacteria; ABF05732; ABF05732; SFV_3711.
DR GeneID; 58389392; -.
DR KEGG; sfv:SFV_3711; -.
DR HOGENOM; CLU_066584_0_0_6; -.
DR OMA; VIVPMGY; -.
DR BioCyc; SFLE373384:SFV_RS20460-MON; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000659; 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_1000062748"
SQ SEQUENCE 359 AA; 40514 MW; 189FA5C7D4C594F3 CRC64;
MTVLIHVLGS DIPHHNRTVL RFFNDALAAT SEHAREFMVV GKDDGLSDSC PALSVQFFPG
KKSLAEAVIA KAKANRQQRF FFHGQFNPTL WLALLSGGIK PSQFFWHIWG ADLYELSSGL
RYKLFYPLRR LAQKRVGCVF ATRGDLSFFA KTHPKVRGEL LYFPTRMDPS LNTMANDRQR
EGKMTILVGN SGDRSNEHVA ALRAVHQQFG DTVKVVVPMG YPPNNEAYIE EVRQAGLELF
SEENLQILSE KLEFDAYLAL LRQCDLGYFI FARQQGIGTL CLLIQAGIPC VLNRENPFWQ
DMTEQHLPVL FTTDDLNEDI VREAQRQLAS ADKNTIAFFS PNYLQGWQRA LAIAAGEVA