YBGC_SHIFL
ID YBGC_SHIFL Reviewed; 134 AA.
AC P0A8Z6; P08999;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Acyl-CoA thioester hydrolase YbgC;
DE Short=Acyl-CoA thioesterase;
DE EC=3.1.2.-;
GN Name=ybgC; OrderedLocusNames=SF0561, S0574;
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: 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}.
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DR EMBL; AE005674; AAN42205.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16078.1; -; Genomic_DNA.
DR RefSeq; NP_706498.1; NC_004337.2.
DR RefSeq; WP_001098384.1; NZ_UIQL01000012.1.
DR AlphaFoldDB; P0A8Z6; -.
DR SMR; P0A8Z6; -.
DR STRING; 198214.SF0561; -.
DR EnsemblBacteria; AAN42205; AAN42205; SF0561.
DR EnsemblBacteria; AAP16078; AAP16078; S0574.
DR GeneID; 1023534; -.
DR GeneID; 67413775; -.
DR KEGG; sfl:SF0561; -.
DR KEGG; sfx:S0574; -.
DR PATRIC; fig|198214.7.peg.650; -.
DR HOGENOM; CLU_101141_7_2_6; -.
DR OMA; YHASYLR; -.
DR OrthoDB; 1786865at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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;
KW Reference proteome.
FT CHAIN 1..134
FT /note="Acyl-CoA thioester hydrolase YbgC"
FT /id="PRO_0000087765"
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