YBGC_ECOL6
ID YBGC_ECOL6 Reviewed; 134 AA.
AC P0A8Z4; P08999;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Acyl-CoA thioester hydrolase YbgC;
DE Short=Acyl-CoA thioesterase;
DE EC=3.1.2.-;
GN Name=ybgC; OrderedLocusNames=c0815;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Thioesterase that appears to be involved in phospholipid
CC metabolism. Some specific acyl-ACPs could be physiological substrates.
CC Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro,
CC catalyzing the hydrolysis of the thioester bond (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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; AE014075; AAN79288.1; -; Genomic_DNA.
DR RefSeq; WP_001098384.1; NC_004431.1.
DR AlphaFoldDB; P0A8Z4; -.
DR SMR; P0A8Z4; -.
DR STRING; 199310.c0815; -.
DR EnsemblBacteria; AAN79288; AAN79288; c0815.
DR GeneID; 67413775; -.
DR KEGG; ecc:c0815; -.
DR eggNOG; COG0824; Bacteria.
DR HOGENOM; CLU_101141_7_2_6; -.
DR OMA; YHASYLR; -.
DR BioCyc; ECOL199310:C0815-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR008272; HB-CoA_thioesterase_AS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR InterPro; IPR014166; Tol-Pal_acyl-CoA_thioesterase.
DR InterPro; IPR006684; YbgC/YbaW.
DR Pfam; PF03061; 4HBT; 1.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR02799; thio_ybgC; 1.
DR TIGRFAMs; TIGR00051; TIGR00051; 1.
DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid metabolism; Membrane.
FT CHAIN 1..134
FT /note="Acyl-CoA thioester hydrolase YbgC"
FT /id="PRO_0000087764"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10041"
SQ SEQUENCE 134 AA; 15562 MW; C44582B6EC3BE989 CRC64;
MNTTLFRWPV RVYYEDTDAG GVVYHASYVA FYERARTEML RHHHFSQQAL MAERVAFVVR
KMTVEYYAPA RLDDMLEIQT EITSMRGTSL VFTQRIVNAE NTLLNEAEVL VVCVDPLKMK
PRALPKSIVA EFKQ