ID   LIP2_STAAU              Reviewed;         690 AA.
AC   P10335;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Lipase 2;
DE            EC=3.1.1.3;
DE   AltName: Full=Glycerol ester hydrolase 2;
DE   Flags: Precursor;
GN   Name=lip2; Synonyms=geh;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3009394; DOI=10.1128/jb.166.2.385-391.1986;
RA   Lee C.Y., Iandolo J.J.;
RT   "Lysogenic conversion of staphylococcal lipase is caused by insertion of
RT   the bacteriophage L54a genome into the lipase structural gene.";
RL   J. Bacteriol. 166:385-391(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 296-307, AND PROTEOLYTIC PROCESSING.
RC   STRAIN=TEN 5;
RX   PubMed=1548232; DOI=10.1128/jb.174.6.1844-1847.1992;
RA   Rollof J., Normark S.;
RT   "In vivo processing of Staphylococcus aureus lipase.";
RL   J. Bacteriol. 174:1844-1847(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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: The expression of Staphylococcus lipase is negatively
CC       regulated by bacteriophage lysogenization (lipase conversion).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M12715; AAA26633.1; -; Genomic_DNA.
DR   PIR; A24545; A24545.
DR   RefSeq; WP_000943836.1; NZ_WOFG01000001.1.
DR   AlphaFoldDB; P10335; -.
DR   SMR; P10335; -.
DR   ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR   PRO; PR:P10335; -.
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; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 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; Secreted; Signal; Zymogen.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   PROPEP          38..295
FT                   /evidence="ECO:0000269|PubMed:1548232"
FT                   /id="PRO_0000017752"
FT   CHAIN           296..690
FT                   /note="Lipase 2"
FT                   /id="PRO_0000017753"
FT   REGION          52..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..690
FT                   /note="Hydrophobic"
FT   COMPBIAS        52..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        603
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        645
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         644
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         647
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         652
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         655
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   690 AA;  76388 MW;  8E8E3654D0E01A3B CRC64;
     MLRGQEERKY SIRKYSIGVV SVLAATMFVV SSHEAQASEK TSTNAAAQKE TLNQPGEQGN
     AITSHQMQSG KQLDDMHKEN GKSGTVTEGK DTLQSSKHQS TQNSKTIRTQ NDNQVKQDSE
     RQGSKQSHQN NATNNTERQN DQVQNTHHAE RNGSQSTTSQ SNDVDKSQPS IPAQKVIPNH
     DKAAPTSTTP PSNDKTAPKS TKAQDATTDK HPNQQDTHQP AHQIIDAKQD DTVRQSEQKP
     QVGDLSKHID GQNSPEKPTD KNTDNKQLIK DALQAPKTRS TTNAAADAKK VRPLKANQVQ
     PLNKYPVVFV HGFLGLVGDN APALYPNYWG GNKFKVIEEL RKQGYNVHQA SVSAFGSNYD
     RAVELYYYIK GGRVDYGAAH AAKYGHERYG KTYKGIMPNW EPGKKVHLVG HSMGGQTIRL
     MEEFLRNGNK EEIAYHKAHG GEISPLFTGG HNNMVASITT LATPHNGSQA ADKFGNTEAV
     RKIMFALNRF MGNKYSNIDL GLTQWGFKQL PNESYIDYIK RVSKSKIWTS DDNAAYDLTL
     DGSAKLNNMT SMNPNITYTT YTGVSSHTGP LGYENPDLGT FFLMATTSRI IGHDAREEWR
     KNDGVVPVIS SLHPSNQPFV NVTNDEPATR RGIWQVKPII QGWDHVDFIG VDFLDFKRKG
     AELANFYTGI INDLLRVEAT ESKGTQLKAS