ID   LIP_PSES5               Reviewed;         364 AA.
AC   P25275;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Triacylglycerol lipase {ECO:0000250|UniProtKB:Q05489};
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:Q05489};
DE   AltName: Full=Extracellular lipase {ECO:0000303|PubMed:1368739};
DE   AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
DE   Flags: Precursor;
GN   Name=lip {ECO:0000303|PubMed:1368739};
OS   Pseudomonas sp. (strain KWI-56).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 45-47.
RX   PubMed=1368739; DOI=10.1271/bbb1961.55.2349;
RA   Iizumi T., Nakamura K., Shimada Y., Sugihara A., Tominaga Y., Fukase T.;
RT   "Cloning, nucleotide sequencing, and expression in Escherichia coli of a
RT   lipase and its activator genes from Pseudomonas sp. KWI-56.";
RL   Agric. Biol. Chem. 55:2349-2357(1991).
CC   -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol.
CC       {ECO:0000250|UniProtKB:Q05489}.
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         Evidence={ECO:0000250|UniProtKB:Q05489};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q05489};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q05489};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q05489}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q05489}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC       family. {ECO:0000305}.
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DR   EMBL; D10069; BAA00960.1; -; Genomic_DNA.
DR   EMBL; S77842; AAC60400.1; -; Genomic_DNA.
DR   AlphaFoldDB; P25275; -.
DR   SMR; P25275; -.
DR   DrugBank; DB03999; Butylphosphonate.
DR   ESTHER; psesp-lipas; Bacterial_lip_FamI.2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002918; Lipase_EstA/Esterase_EstB.
DR   PANTHER; PTHR32015; PTHR32015; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000269|PubMed:1368739"
FT   CHAIN           45..364
FT                   /note="Triacylglycerol lipase"
FT                   /id="PRO_0000017745"
FT   DOMAIN          54..333
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   ACT_SITE        308
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   ACT_SITE        330
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22088"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22088"
FT   BINDING         286
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   BINDING         332
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   BINDING         340
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
FT   DISULFID        234..314
FT                   /evidence="ECO:0000250|UniProtKB:Q05489"
SQ   SEQUENCE   364 AA;  37511 MW;  F346CB8B2E94E27D CRC64;
     MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPADGYAA TRYPIILVHG
     LSGTDKYAGV VEYWYGIQED LQQNGATVYV ANLSGFQSDD GANGRGEQLL AYVKTVLAAT
     GATKVNLVGH SQGGLTSRYV AAVAPDLVAS VTTIGTPHRG SEFADFVQNV LAYDPTGLSS
     SVIAAFVNVF GILTSSSHNT NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT
     ETVGGNTHLL YSWAGTAIQP TLSVFGITGA TDTSTVPLVD LANVLDPSTL ALFGTGTVMI
     NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA VIRTHANRLK
     LAGV