ID   LIP2_STAA8              Reviewed;         690 AA.
AC   Q2G155;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=SAOUHSC_00300;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=RN4220;
RX   PubMed=20472795; DOI=10.1128/jb.01452-09;
RA   Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA   Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA   van Dijl J.M.;
RT   "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 192:3788-3800(2010).
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:0000269|PubMed:20472795}.
CC   -!- INDUCTION: Less protein is secreted in a secG or double secG/secY2
CC       mutant (at protein level). {ECO:0000269|PubMed:20472795}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD29469.1; -; Genomic_DNA.
DR   RefSeq; WP_000943836.1; NZ_LS483365.1.
DR   RefSeq; YP_498890.1; NC_007795.1.
DR   AlphaFoldDB; Q2G155; -.
DR   SMR; Q2G155; -.
DR   STRING; 1280.SAXN108_0305; -.
DR   ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR   PRIDE; Q2G155; -.
DR   EnsemblBacteria; ABD29469; ABD29469; SAOUHSC_00300.
DR   GeneID; 3919527; -.
DR   KEGG; sao:SAOUHSC_00300; -.
DR   PATRIC; fig|93061.5.peg.273; -.
DR   eggNOG; COG1075; Bacteria.
DR   eggNOG; COG3087; Bacteria.
DR   HOGENOM; CLU_023555_2_0_9; -.
DR   OMA; DNMVASI; -.
DR   PRO; PR:Q2G155; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..690
FT                   /note="Lipase 2"
FT                   /id="PRO_0000414598"
FT   REGION          52..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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="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"
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