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WECF_SHIFL
ID   WECF_SHIFL              Reviewed;         359 AA.
AC   Q83PH8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SF3867, S3893;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45304.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18894.1; -; Genomic_DNA.
DR   RefSeq; NP_709597.1; NC_004337.2.
DR   RefSeq; WP_000217247.1; NZ_WPGW01000028.1.
DR   AlphaFoldDB; Q83PH8; -.
DR   SMR; Q83PH8; -.
DR   STRING; 198214.SF3867; -.
DR   EnsemblBacteria; AAN45304; AAN45304; SF3867.
DR   EnsemblBacteria; AAP18894; AAP18894; S3893.
DR   GeneID; 1025968; -.
DR   GeneID; 58389392; -.
DR   KEGG; sfl:SF3867; -.
DR   KEGG; sfx:S3893; -.
DR   PATRIC; fig|198214.7.peg.4557; -.
DR   HOGENOM; CLU_066584_0_0_6; -.
DR   OMA; VIVPMGY; -.
DR   OrthoDB; 1834836at2; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000216189"
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
 
 
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