ID   AES_ECO8A               Reviewed;         319 AA.
AC   B7M3W8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=ECIAI1_0479;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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: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; CU928160; CAQ97351.1; -; Genomic_DNA.
DR   RefSeq; WP_000801838.1; NC_011741.1.
DR   AlphaFoldDB; B7M3W8; -.
DR   SMR; B7M3W8; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR   MEROPS; S09.A47; -.
DR   KEGG; ecr:ECIAI1_0479; -.
DR   HOGENOM; CLU_012494_6_4_6; -.
DR   OMA; LWYPSTM; -.
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; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN           1..319
FT                   /note="Acetyl esterase"
FT                   /id="PRO_1000188981"
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   319 AA;  36038 MW;  C4163606744F7930 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPS WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKIAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL