ID   LIP1_STAA8              Reviewed;         680 AA.
AC   Q2FUU5;
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 1;
DE            EC=3.1.1.3;
DE   AltName: Full=Glycerol ester hydrolase 1;
DE   Flags: Precursor;
GN   Name=lipA; OrderedLocusNames=SAOUHSC_03006;
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=ISP479C;
RX   PubMed=18621893; DOI=10.1128/jb.00300-08;
RA   Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT   "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL   J. Bacteriol. 190:6188-6196(2008).
RN   [3]
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:18621893,
CC       ECO:0000269|PubMed:20472795}.
CC   -!- INDUCTION: Less protein is secreted in a secA2 or a double secG/secY2
CC       mutant (at protein level). {ECO:0000269|PubMed:18621893,
CC       ECO:0000269|PubMed:20472795}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD31993.1; -; Genomic_DNA.
DR   RefSeq; WP_000842036.1; NZ_LS483365.1.
DR   RefSeq; YP_501455.1; NC_007795.1.
DR   AlphaFoldDB; Q2FUU5; -.
DR   SMR; Q2FUU5; -.
DR   STRING; 1280.SAXN108_2943; -.
DR   ESTHER; staau-LIP; Bacterial_lip_FamI.6.
DR   EnsemblBacteria; ABD31993; ABD31993; SAOUHSC_03006.
DR   GeneID; 3921488; -.
DR   KEGG; sao:SAOUHSC_03006; -.
DR   PATRIC; fig|93061.5.peg.2714; -.
DR   eggNOG; COG1075; Bacteria.
DR   HOGENOM; CLU_023555_2_1_9; -.
DR   OMA; NGYEAYE; -.
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..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..290
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000414596"
FT   CHAIN           291..680
FT                   /note="Lipase 1"
FT                   /id="PRO_0000414597"
FT   REGION          82..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        408
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        639
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
SQ   SEQUENCE   680 AA;  76675 MW;  F91CD0F8648263E7 CRC64;
     MKSQNKYSIR KFSVGASSIL IATLLFLSGG QAQAAEKQVN MGNSQEDTVT AQSIGDQQTR
     ENANYQRENG VDEQQHTENL TKNLHNDKTI SEENHRKTDD LNKDQLKDDK KSSLNNKNIQ
     RDTTKNNNAN PSDVNQGLEQ AINDGKQSKV ASQQQSKEAD NSQDSNANNN LPSQSRIKEA
     PSLNKLDQTS QREIVNETEI EKVQPQQNNQ ANDKITNYNF NNEQEVKPQK DEKTLSVSDL
     KNNQKSPVEP TKDNDKKNGL NLLKSSAVAT LPNKGTKELT AKAKDDQTNK VAKQGQYKNQ
     DPIVLVHGFN GFTDDINPSV LAHYWGGNKM NIRQDLEENG YKAYEASISA FGSNYDRAVE
     LYYYIKGGRV DYGAAHAAKY GHERYGKTYE GIYKDWKPGQ KVHLVGHSMG GQTIRQLEEL
     LRNGNREEIE YQKKHGGEIS PLFKGNHDNM ISSITTLGTP HNGTHASDLA GNEALVRQIV
     FDIGKMFGNK NSRVDFGLAQ WGLKQKPNES YIDYVKRVKQ SNLWKSKDNG FYDLTREGAT
     DLNRKTSLNP NIVYKTYTGE ATHKALNSDR QKADLNMFFP FVITGNLIGK ATEKEWREND
     GLVSVISSQH PFNQAYTKAT DKIQKGIWQV TPTKHDWDHV DFVGQDSSDT VRTREELQDF
     WHHLADDLVK TEKLTDTKQA