ID AES_SALSV Reviewed; 323 AA.
AC B4TMG8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Acetyl esterase {ECO:0000255|HAMAP-Rule:MF_01958};
DE EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_01958};
GN Name=aes {ECO:0000255|HAMAP-Rule:MF_01958}; OrderedLocusNames=SeSA_A0552;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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:0000255|HAMAP-Rule:MF_01958}.
CC -!- SUBUNIT: Homodimer. Interacts with MalT and MelA. {ECO:0000255|HAMAP-
CC Rule:MF_01958}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01958}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01958}.
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DR EMBL; CP001127; ACF92921.1; -; Genomic_DNA.
DR RefSeq; WP_000801785.1; NC_011094.1.
DR AlphaFoldDB; B4TMG8; -.
DR SMR; B4TMG8; -.
DR ESTHER; salty-AES; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR KEGG; sew:SeSA_A0552; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR Proteomes; UP000001865; 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; Hydrolase; Serine esterase.
FT CHAIN 1..323
FT /note="Acetyl esterase"
FT /id="PRO_1000188995"
FT MOTIF 91..93
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
FT ACT_SITE 262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
FT ACT_SITE 292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
SQ SEQUENCE 323 AA; 36811 MW; 3E28CE92BA06E75A CRC64;
MKPENKIPVL TRLSDEMTAV VNFQQPGLPP WPADGDIETQ RQYYLLERRF WNADAPSMTT
RTCAVPTPYG DVTTRLYSPQ PTSQAILYYL HGGGFILGNL DTHDRIMRLL ARYTGCTVIG
IDYSLSPQAR YPQAIEETVA VCSYFSQHAD EYSLNVEKIG FAGDSAGAML ALASALWLRD
KHIRCGNVIA ILLWYGLYGL QDSVSRRLFG GAWDGLTRED LDMYEKAYLR NEDDRESPWY
CLFNNDLTRD VPPCFIASAE FDPLIDDSRL LHQTLQAHQQ PCEYKMYPGT LHAFLHYSRM
MTIADDALQD GARFFMARMK TPR
//
