ID   LIPA_PSEFL              Reviewed;         449 AA.
AC   P26504;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, 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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=SIK W1;
RX   PubMed=1368740; DOI=10.1271/bbb1961.55.2359;
RA   Chung G.H., Lee Y.P., Jeohn G.H., Yoo O.J., Rhee J.S.;
RT   "Cloning and nucleotide sequence of thermostable lipase gene from
RT   Pseudomonas fluorescens SIK W1.";
RL   Agric. Biol. Chem. 55:2359-2365(1991).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; S77830; AAC60402.1; -; Genomic_DNA.
DR   EMBL; D11455; BAA02012.1; -; Genomic_DNA.
DR   PIR; JQ1277; JQ1277.
DR   AlphaFoldDB; P26504; -.
DR   SMR; P26504; -.
DR   ESTHER; psefl-siklip; Bacterial_lip_FamI.3.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..449
FT                   /note="Lipase"
FT                   /id="PRO_0000017742"
FT   REPEAT          372..389
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          390..407
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REGION          58..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         318
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         387
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  48233 MW;  16E539323D5D0DD8 CRC64;
     MGVFDYKNLG TEASKTLFAD ATAITLYTYH NLDNGFAVGY QQHGLGLGCR HTGRGVARQH
     RLPGSDPPAF PGILTRKRPP WTRCTQPVGR QSSASALGYG GKVDARGTFF GEKAGYTTAQ
     AEVLGKYDDA GKLLEIGIGF RGTSGPRESL ITTPCRSGQR PARRAGPQGL CEKLCRRTFG
     GLLKTVADYA GAHGLSGKDV LVSGHSLGGL AVNSMADLST SKWAGFYKDA NYLAYASPTQ
     SAGDKVLNIG YENDPVFRAL DGSTFNLSSL GVHDKAHEST TDNIVSFNDH YASTLWNVLP
     FSIANLSTWV SHLPSAYGDG MTRVLESGFY EQMTRDSTII LCPTWSDPAR ANTWVQDLNR
     NAEPHTGNTF IIGSDGNDLI QGGKGADFIE GGKGNDTIRD NSGHNTFLFS GHFGQDRIIG
     YQPTGWCSRA PTAAPTCATT RRPWGPIRC