ID   AES_ECOBW               Reviewed;         319 AA.
AC   C4ZUT0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=BWG_0357;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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; CP001396; ACR61905.1; -; Genomic_DNA.
DR   RefSeq; WP_000801813.1; NC_012759.1.
DR   AlphaFoldDB; C4ZUT0; -.
DR   SMR; C4ZUT0; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR   MEROPS; S09.A47; -.
DR   KEGG; ebw:BWG_0357; -.
DR   HOGENOM; CLU_012494_6_4_6; -.
DR   OMA; LWYPSTM; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR   GO; GO:0008126; F:acetylesterase activity; IDA:CAFA.
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_1000216210"
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;  36034 MW;  4F9E234E23CCE7D0 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL