(data stored in ACNUC10821 zone)

SWISSPROT: C8U2G2_ECO10

ID   C8U2G2_ECO10            Unreviewed;       319 AA.
AC   C8U2G2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
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   ECO:0000313|EMBL:BAI29320.1};
GN   OrderedLocusNames=ECO103_0452 {ECO:0000313|EMBL:BAI29320.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29320.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29320.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Displays esterase activity towards short chain fatty
CC       esters (acyl chain length of up to 8 carbons). Able to hydrolyze
CC       triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin),
CC       but not trioleylglycerol (triolein) or cholesterol oleate.
CC       Negatively regulates MalT activity by antagonizing maltotriose
CC       binding. Inhibits MelA galactosidase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01958}.
CC   -!- SUBUNIT: Homodimer. Interacts with MalT and MelA.
CC       {ECO:0000256|HAMAP-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; AP010958; BAI29320.1; -; Genomic_DNA.
DR   RefSeq; WP_000801832.1; NC_013353.1.
DR   SMR; C8U2G2; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR   EnsemblBacteria; BAI29320; BAI29320; ECO103_0452.
DR   KEGG; eoh:ECO103_0452; -.
DR   HOGENOM; HOG000117644; -.
DR   KO; K01066; -.
DR   OMA; HPFIAMD; -.
DR   BioCyc; ECOL585395:ECO103_RS02365-MONOMER; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U2G2.
DR   SWISS-2DPAGE; C8U2G2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01958};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01958};
KW   Serine esterase {ECO:0000256|HAMAP-Rule:MF_01958}.
FT   DOMAIN       87    295       Abhydrolase_3. {ECO:0000259|Pfam:
FT                                PF07859}.
FT   ACT_SITE    165    165       {ECO:0000256|HAMAP-Rule:MF_01958,
FT                                ECO:0000256|PROSITE-ProRule:PRU10038}.
FT   ACT_SITE    262    262       {ECO:0000256|HAMAP-Rule:MF_01958}.
FT   ACT_SITE    292    292       {ECO:0000256|HAMAP-Rule:MF_01958}.
SQ   SEQUENCE   319 AA;  36034 MW;  68C23311A68CA827 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPS WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYPLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKIAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL
//

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