AES_ECO27
ID AES_ECO27 Reviewed; 319 AA.
AC B7UKF6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=E2348C_0411;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(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; FM180568; CAS07959.1; -; Genomic_DNA.
DR RefSeq; WP_000801821.1; NC_011601.1.
DR AlphaFoldDB; B7UKF6; -.
DR SMR; B7UKF6; -.
DR ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR EnsemblBacteria; CAS07959; CAS07959; E2348C_0411.
DR KEGG; ecg:E2348C_0411; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR OMA; LWYPSTM; -.
DR Proteomes; UP000008205; 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; 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_1000188975"
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; 36103 MW; 344A1F65AD6D82D4 CRC64;
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNVGAPEMAT
RAYRVPTKYG QVKTRIFYPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
MKTADEALLD GAQFFTAQL
