ID C3TL92_ECOLX Unreviewed; 319 AA.
AC C3TL92;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Acetyl esterase {ECO:0000256|HAMAP-Rule:MF_01958};
DE EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_01958};
GN Name=aes {ECO:0000256|HAMAP-Rule:MF_01958};
GN ORFNames=C9E67_23285 {ECO:0000313|EMBL:QCL49802.1}, ECs0529
GN {ECO:0000313|EMBL:ACI87476.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI87476.1};
RN [1] {ECO:0000313|EMBL:ACI87476.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI87476.1}, 86-24
RC {ECO:0000313|EMBL:ACI87477.1}, 87-14 {ECO:0000313|EMBL:ACI87478.1},
RC and TW14359 {ECO:0000313|EMBL:ACI87480.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL49802.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL49802.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01958}.
CC -!- SUBUNIT: Homodimer. Interacts with MalT and MelA. {ECO:0000256|HAMAP-
CC Rule:MF_01958}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01958}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|HAMAP-Rule:MF_01958}.
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DR EMBL; EU904930; ACI87476.1; -; Genomic_DNA.
DR EMBL; EU904931; ACI87477.1; -; Genomic_DNA.
DR EMBL; EU904932; ACI87478.1; -; Genomic_DNA.
DR EMBL; EU904934; ACI87480.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL49802.1; -; Genomic_DNA.
DR RefSeq; WP_000801803.1; NZ_VODI01000075.1.
DR ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR PATRIC; fig|562.7073.peg.839; -.
DR OMA; LWYPSTM; -.
DR Proteomes; UP000298553; 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; alpha/beta hydrolase; 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 PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01958};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01958};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01958}.
FT DOMAIN 87..295
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 165
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 262
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958"
FT ACT_SITE 292
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01958"
SQ SEQUENCE 319 AA; 36034 MW; 508621C1DCD4E8DD CRC64;
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
KAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
IDYTLSPEAR FPQVIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
MKTADEALRD GAQFFTAQL
//
