WECF_SALPB
ID WECF_SALPB Reviewed; 359 AA.
AC A9MXG5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-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=SPAB_04872;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000886; ABX70176.1; -; Genomic_DNA.
DR RefSeq; WP_000217188.1; NC_010102.1.
DR AlphaFoldDB; A9MXG5; -.
DR CAZy; GT56; Glycosyltransferase Family 56.
DR KEGG; spq:SPAB_04872; -.
DR PATRIC; fig|1016998.12.peg.4580; -.
DR HOGENOM; CLU_066584_0_0_6; -.
DR OMA; VIVPMGY; -.
DR BioCyc; SENT1016998:SPAB_RS19815-MON; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000008556; 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_1000083951"
SQ SEQUENCE 359 AA; 40471 MW; B09F11EAB33F1D58 CRC64;
MTVLIHVLGS DIPHHNHTVL RFFNDTLAAT SEHAREFMVA GEDNGFTESC PALSLRFYGS
KKALAQAVIA KAKANRRQRF FFHGQFNTSL WLALLSGGIK PAQFYWHIWG ADLYEVSHGL
KFRLFYPLRR IAQGRVGGVF ATRGDLSYFA RQHPGVRGEL LYFPTRMDPS LNAMAKERQR
AGKLTILVGN SGDRSNQHIA ALRAVYQQFG DTVNVVVPMG YPANNQAYID EVRQAGLALF
SAENLQILSE KMEFDTYLAL LRQCDLGYFI FARQQGIGTL CLLIQADIPC VLNRDNPFWQ
DMAEQHLPVL FTTDDLNEQV VREAQRQLAS VDKSGITFFS PNYLQPWHNA LRIAAGEAE