ID   LIP2_STAAW              Reviewed;         690 AA.
AC   Q8NYC2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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; OrderedLocusNames=MW0297;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB94162.1; -; Genomic_DNA.
DR   RefSeq; WP_000943814.1; NC_003923.1.
DR   AlphaFoldDB; Q8NYC2; -.
DR   SMR; Q8NYC2; -.
DR   ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR   EnsemblBacteria; BAB94162; BAB94162; BAB94162.
DR   KEGG; sam:MW0297; -.
DR   HOGENOM; CLU_023555_2_0_9; -.
DR   OMA; DNMVASI; -.
DR   Proteomes; UP000000418; Chromosome.
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   3: Inferred from homology;
KW   Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   PROPEP          38..295
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000017754"
FT   CHAIN           296..690
FT                   /note="Lipase 2"
FT                   /id="PRO_0000017755"
FT   REGION          53..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..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;  76522 MW;  36FFB5E0BB434CCA CRC64;
     MLRGQEERKY SIRKYSIGVV SVLAATMFVV SSHEAQASEK TPTNAAVQKE TLNQPGEQGN
     AITSHQMQSG KQLDDMHKEN GKSGTVTEGK DTLQLSKYQS TQNSKTIRTQ NDNQVKQDSE
     RQGSKQSHQN NATNNTERQN DQVQNTHHAE RNGSQSTTSQ SNDVDKSQPS IPAQKVLPNH
     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 FFLMDTTSRI IGHDAREEWR
     KNDGVVPVIS SLHPSNQPFV NVTNDEPATR RGIWQVKPII QGWDHVDFIG VDFLDFKRKG
     AELANFYTGI INDLLRVEAT ESKGTQLKAS