ID   EST_ACIVR               Reviewed;         303 AA.
AC   P18773;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Esterase;
DE            EC=3.1.1.-;
GN   Name=est;
OS   Acinetobacter venetianus (strain ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG
OS   45561 / CIP 110063 / KCTC 2702 / LMG 19082 / RAG-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1191460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG 45561 / CIP 110063 / KCTC
RC   2702 / LMG 19082 / RAG-1;
RX   PubMed=2545531; DOI=10.1016/0378-1119(89)90016-4;
RA   Reddy P.G., Allon R., Mevarech M., Mendelovitz S., Sato Y., Gutnick D.L.;
RT   "Cloning and expression in Escherichia coli of an esterase-coding gene from
RT   the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1.";
RL   Gene 76:145-152(1989).
RN   [2]
RP   SEQUENCE REVISION.
RA   Gutnick D.L.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=External to the
CC       cytoplasmic membrane.
CC   -!- MISCELLANEOUS: Acinetobacter lwoffii RAG-1 has the ability to grow on
CC       simple triglycerides such as triacetin; mutants defective in esterase
CC       lose this ability, but retain the ability to grow on acetate.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; M24890; AAA02895.1; -; Genomic_DNA.
DR   PIR; JS0202; JS0202.
DR   AlphaFoldDB; P18773; -.
DR   SMR; P18773; -.
DR   ESTHER; acica-este1; Hormone-sensitive_lipase_like.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
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   Hydrolase; Secreted; Serine esterase.
FT   CHAIN           1..303
FT                   /note="Esterase"
FT                   /id="PRO_0000071554"
FT   MOTIF           79..81
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        149
FT                   /evidence="ECO:0000250|UniProtKB:O06350,
FT                   ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
SQ   SEQUENCE   303 AA;  33911 MW;  3B038A5A15BA81B3 CRC64;
     MKFGTVWKYY FTESLLKATI RTPSQLNLAP NALRPVLDQL CRLFPQNPTV QIRPIRLAGV
     RGEEIKAQAS ATQLIFHIHG GAFFLGSLNT HRALMTDLAS RTQMQVIHVD YPLAPEHPYP
     EAIDAIFDVY QALLVQGIKP KDIIISGDSC GANLALALSL RLKQQPELMP SGLILMSPYL
     DLTLTSESLR FNQKHDALLS IEALQAGIKH YLTDDIQPGD PRVSPLFDDL DGLPPTLVQV
     GSKEILLDDS KRFREKAEQA DVKVHFKLYT GMWNNFQMFN AWFPEAKQAL ADIAEFATSL
     DLD