ID C0PVE2_SALPC Unreviewed; 332 AA.
AC C0PVE2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Acetyl esterase {ECO:0000256|HAMAP-Rule:MF_01958};
DE EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_01958};
GN Name=aes {ECO:0000256|HAMAP-Rule:MF_01958,
GN ECO:0000313|EMBL:ACN44685.1};
GN OrderedLocusNames=SPC_0505 {ECO:0000313|EMBL:ACN44685.1};
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN44685.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN44685.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN44685.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Displays esterase activity towards short chain fatty esters
CC (acyl chain length of up to 8 carbons). Able to hydrolyze
CC triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but
CC not trioleylglycerol (triolein) or cholesterol oleate. Negatively
CC regulates MalT activity by antagonizing maltotriose binding. Inhibits
CC MelA galactosidase activity. {ECO:0000256|HAMAP-Rule:MF_01958}.
CC -!- SUBUNIT: Homodimer. Interacts with MalT and MelA. {ECO:0000256|HAMAP-
CC Rule:MF_01958}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01958}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|HAMAP-Rule:MF_01958}.
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; CP000857; ACN44685.1; -; Genomic_DNA.
DR AlphaFoldDB; C0PVE2; -.
DR ESTHER; salty-AES; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR KEGG; sei:SPC_0505; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR Proteomes; UP000001599; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR HAMAP; MF_01958; Acetyl_esterase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR023508; Acetyl_esterase.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01958};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01958};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01958}.
FT DOMAIN 97..304
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 174
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 271
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958"
FT ACT_SITE 301
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958"
SQ SEQUENCE 332 AA; 38022 MW; 6E865119E83A8FC9 CRC64;
MVHFHKERFM KPENKIPVLT RLSDEMKAVV NFQQPGLPPW PADGDIETQR QYYLLERRFW
NADAPSMTTR TCAVPTPYGD VTTRLYSPQP TSQAALYYLH GGGFILGNLD THDRIMRLLA
RYTGCTVIGI DYSLSPQARY PQAIEETVAV CSYFSQHADE YSLNVEKIGF AGDSAGAMLA
LASALWLRDK HIRCGNLIAI LLWYGLYGLQ DSVSRRLFGG AWDGLTREDL DMYEKAYLRN
DEDRESPWYC LFNNDLTRDV PPCFIASAEF DPLIDDSRLL HQTLQAHQQP CEYKMYPGTL
HAFLHYSRMM TIADDALQDG ARFFMARMKT PR
//
