ID   LIPB_PSEFL              Reviewed;         476 AA.
AC   P41773;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Lipase;
DE            EC=3.1.1.3;
DE   AltName: Full=Triacylglycerol lipase;
DE   Flags: Precursor;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B52;
RX   PubMed=1599260; DOI=10.1128/aem.58.4.1402-1407.1992;
RA   Tan Y., Miller K.J.;
RT   "Cloning, expression, and nucleotide sequence of a lipase gene from
RT   Pseudomonas fluorescens B52.";
RL   Appl. Environ. Microbiol. 58:1402-1407(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M86350; AAA25882.1; -; Genomic_DNA.
DR   PIR; A43942; A43942.
DR   AlphaFoldDB; P41773; -.
DR   SMR; P41773; -.
DR   STRING; 690597.JH730929_gene1868; -.
DR   ESTHER; psefl-lipb; Bacterial_lip_FamI.3.
DR   eggNOG; COG2931; Bacteria.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF00353; HemolysinCabind; 1.
DR   SUPFAM; SSF51120; SSF51120; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   3: Inferred from homology;
KW   Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..476
FT                   /note="Lipase"
FT                   /id="PRO_0000017743"
FT   REPEAT          372..389
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          390..407
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REPEAT          410..427
FT                   /note="Hemolysin-type calcium-binding 3"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         437
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  50239 MW;  FC38C080F0A3BC55 CRC64;
     MGIFDYKNLG TEGSKTLFAD AMAITLYSYH NLDNGFAVGY QHNGLGLGLP ATLVGALLGS
     TDSQGVIPGI PWNPDSEKAA LEAVQKAGWT PISASALGYA GKVDARGTFF GEKAGYTTAQ
     VEVLGKYDDA GKLLEIGIGF RGTSGPRETL ISDSIGDLIS DLLAALGPKD YAKNYAGEAF
     GGLLKNVADY AGAHGLTGKD VVVSGHSLGG LAVNSMADLS NYKWAGFYKD ANYVAYASPT
     QSAGDKVLNI GYENDPVFRA LDGSSFNLSS LGVHDKPHES TTDNIVSFND HYASTLWNVL
     PFSIVNLPTW VSHLPTAYGD GMTRILESGF YDQMTRDSTV IVANLSDPAR ANTWVQDLNR
     NAEPHKGNTF IIGSDGNDLI QGGNGADFIE GGKGNDTIRD NSGHNTFLFS GHFGNDRVIG
     YQPTDKLVFK DVQGSTDLRD HAKVVGADTV LTFGADSVTL VGVGHGGLWT EGVVIG