ID   AES_SALCH               Reviewed;         323 AA.
AC   Q57S73;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=SCH_0532;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64438.1; -; Genomic_DNA.
DR   RefSeq; WP_001539341.1; NC_006905.1.
DR   AlphaFoldDB; Q57S73; -.
DR   SMR; Q57S73; -.
DR   ESTHER; salty-AES; Hormone-sensitive_lipase_like.
DR   EnsemblBacteria; AAX64438; AAX64438; SCH_0532.
DR   KEGG; sec:SCH_0532; -.
DR   HOGENOM; CLU_012494_6_4_6; -.
DR   OMA; LWYPSTM; -.
DR   Proteomes; UP000000538; 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; -; 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   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 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_0000239708"
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;  36840 MW;  744D4F12AF8C6C21 CRC64;
     MKPENKIPVL TRLSDEMKAV VNFQQPGLPP WPADGDIETQ RQYYLLERRF WNADAPSMTT
     RTCAVPTPYG DVTTRLYSPQ PTSQATLYYL HGGGFILGNL DTHDRIMRLL ARYTGCTVIG
     IDYSLSPQAR YPQAIEETVA VCSYFSQHAD EYSLNVEKIG FAGDSAGAML ALASALWLRD
     KHIRCGNLIA ILLWYGLYGL QDSVSRRLFG GAWDGLTRED LDMYEKAYLR NDEDRESPWY
     CLFNNDLTRD VPPCFIASAE FDPLIDDSRL LHQTLQAHQQ PCEYKMYPGT LHAFLHYSRM
     MTIADDALQD GARFFMARMK TPR