ID   AES_SALTI               Reviewed;         323 AA.
AC   Q8Z8T1; Q7C8B2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 109.
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};
GN   OrderedLocusNames=STY0534, t2370;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD04975.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69961.1; -; Genomic_DNA.
DR   RefSeq; NP_455086.1; NC_003198.1.
DR   RefSeq; WP_000801788.1; NZ_WSUR01000008.1.
DR   AlphaFoldDB; Q8Z8T1; -.
DR   SMR; Q8Z8T1; -.
DR   STRING; 220341.16501761; -.
DR   ESTHER; salty-AES; Hormone-sensitive_lipase_like.
DR   MEROPS; S09.A47; -.
DR   EnsemblBacteria; AAO69961; AAO69961; t2370.
DR   KEGG; stt:t2370; -.
DR   KEGG; sty:STY0534; -.
DR   PATRIC; fig|220341.7.peg.537; -.
DR   eggNOG; COG0657; Bacteria.
DR   HOGENOM; CLU_012494_6_4_6; -.
DR   OMA; LWYPSTM; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000239710"
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;  36790 MW;  E0BFCF7271781C71 CRC64;
     MKPENKIPVL TRLSDEMTAV VNFQQPGLPP WPADGDIETQ RQYYLLERRF WNADAPSMTT
     RTCAVSTPYG DVTTRLYSPQ PTSQATLYYL HGGGFILGNL DTHDRIMRLL ARYTGCTVIG
     IDYSLSPQAR YPQAIEETVA VCSYFSQHAD EYSLNVEEIG FAGDSAGAML ALASALWLRD
     KHIRCGNVIA ILLWYGLYGL QDSVSRRLFG GAWDGLTRED LDMYEKAYLR NDEDRESPWY
     CLFNNDLTRD VPPCFIASAE FDPLIDDSRL LHQTLQAHQQ PCEYKMYPGT LHAFLHYSRM
     MTIADDALQD GARFFMARMK TPR