WECH_ECOLI
ID WECH_ECOLI Reviewed; 331 AA.
AC P37669; Q2M7M4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=O-acetyltransferase WecH {ECO:0000255|HAMAP-Rule:MF_01949, ECO:0000303|PubMed:16936038};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01949, ECO:0000305|PubMed:16936038};
GN Name=wecH {ECO:0000255|HAMAP-Rule:MF_01949, ECO:0000303|PubMed:16936038};
GN Synonyms=yiaH; OrderedLocusNames=b3561, JW3533;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=16936038; DOI=10.1128/jb.00783-06;
RA Kajimura J., Rahman A., Hsu J., Evans M.R., Gardner K.H., Rick P.D.;
RT "O acetylation of the enterobacterial common antigen polysaccharide is
RT catalyzed by the product of the yiaH gene of Escherichia coli K-12.";
RL J. Bacteriol. 188:7542-7550(2006).
CC -!- FUNCTION: Responsible for the incorporation of O-acetyl groups into the
CC enterobacterial common antigen (ECA) trisaccharide repeat units.
CC Catalyzes the acetylation of both cyclic ECA (ECA(CYC)) and
CC phosphoglyceride-linked ECA (ECA(PG)). {ECO:0000269|PubMed:16936038}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01949,
CC ECO:0000269|PubMed:16936038}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01949, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01949}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in the incorporation of O-
CC acetyl groups into both ECA(CYC) and ECA(PG).
CC {ECO:0000269|PubMed:16936038}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01949, ECO:0000305}.
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DR EMBL; U00039; AAB18538.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76585.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77732.1; -; Genomic_DNA.
DR PIR; S47782; S47782.
DR RefSeq; NP_418018.1; NC_000913.3.
DR RefSeq; WP_001182650.1; NZ_SSZK01000041.1.
DR AlphaFoldDB; P37669; -.
DR SMR; P37669; -.
DR BioGRID; 4262152; 1.
DR BioGRID; 852385; 1.
DR DIP; DIP-12403N; -.
DR IntAct; P37669; 1.
DR STRING; 511145.b3561; -.
DR TCDB; 9.B.97.1.1; the acyltransferase-3/putative acetyl-coa transporter (atat) family.
DR PaxDb; P37669; -.
DR PRIDE; P37669; -.
DR EnsemblBacteria; AAC76585; AAC76585; b3561.
DR EnsemblBacteria; BAE77732; BAE77732; BAE77732.
DR GeneID; 948077; -.
DR KEGG; ecj:JW3533; -.
DR KEGG; eco:b3561; -.
DR PATRIC; fig|1411691.4.peg.3151; -.
DR EchoBASE; EB2183; -.
DR eggNOG; COG3274; Bacteria.
DR HOGENOM; CLU_047714_3_0_6; -.
DR OMA; TFYYVLY; -.
DR PhylomeDB; P37669; -.
DR BioCyc; EcoCyc:EG12274-MON; -.
DR BRENDA; 3.1.8.1; 2165.
DR UniPathway; UPA00566; -.
DR PRO; PR:P37669; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016413; F:O-acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
DR HAMAP; MF_01949; Acetyltr_WecH; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR032905; WecH.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="O-acetyltransferase WecH"
FT /id="PRO_0000208098"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 34..45
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 67..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 100..113
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 135..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 160..168
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 190..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 224..234
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 256..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 288..299
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01949"
FT TOPO_DOM 321..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 331 AA; 37570 MW; 88FD5A182110F63C CRC64;
MQPKIYWIDN LRGIACLMVV MIHTTTWYVT NAHSVSPVTW DIANVLNSAS RVSVPLFFMI
SGYLFFGERS AQPRHFLRIG LCLIFYSAIA LLYIALFTSI NMELALKNLL QKPVFYHLWF
FFAIAVIYLV SPLIQVKNVG GKMLLVLMAV IGIIANPNTV PQKIDGFEWL PINLYINGDT
FYYILYGMLG RAIGMMDTQH KALSWVSAAL FATGVFIISR GTLYELQWRG NFADTWYLYC
GPMVFICAIA LLTLVKNTLD TRTIRGLGLI SRHSLGIYGF HALIIHALRT RGIELKNWPI
LDIIWIFCAT LAASLLLSML VQRIDRNRLV S
