AES_ECO24
ID AES_ECO24 Reviewed; 319 AA.
AC A7ZIN6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=EcE24377A_0514;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV20987.1; -; Genomic_DNA.
DR RefSeq; WP_000801847.1; NC_009801.1.
DR AlphaFoldDB; A7ZIN6; -.
DR SMR; A7ZIN6; -.
DR ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR SwissPalm; A7ZIN6; -.
DR EnsemblBacteria; ABV20987; ABV20987; EcE24377A_0514.
DR KEGG; ecw:EcE24377A_0514; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR OMA; LWYPSTM; -.
DR Proteomes; UP000001122; 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_1000188974"
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; 36054 MW; C1C09FE2674CF064 CRC64;
MKPENKLPVL DLISAEMKTV VNTLQSDLPS WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
IDYPLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML TLASALWLRD
KQIDCGKIAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
MKTADEALRD GAQFFTAQL
