ID   LIP1_STAAN              Reviewed;         680 AA.
AC   P65289; Q99QX0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   AltName: Full=Glycerol ester hydrolase 1;
DE   Flags: Precursor;
GN   Name=lip1; OrderedLocusNames=SA2463;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB43769.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000018; BAB43769.1; ALT_INIT; Genomic_DNA.
DR   PIR; G90075; G90075.
DR   RefSeq; WP_000842040.1; NC_002745.2.
DR   AlphaFoldDB; P65289; -.
DR   SMR; P65289; -.
DR   ESTHER; staau-LIP; Bacterial_lip_FamI.6.
DR   EnsemblBacteria; BAB43769; BAB43769; BAB43769.
DR   KEGG; sau:SA2463; -.
DR   HOGENOM; CLU_023555_2_1_9; -.
DR   OMA; NGYEAYE; -.
DR   Proteomes; UP000000751; 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..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..290
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000017750"
FT   CHAIN           291..680
FT                   /note="Lipase 1"
FT                   /id="PRO_0000017751"
FT   REGION          82..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        600
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"
FT   BINDING         638
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         641
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         646
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         649
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   680 AA;  76531 MW;  9F670E795C08C61F CRC64;
     MKSQNKYSIR KFSVGASSIL IATLLFLSGG QAQAAEKQVN MGNSQEDTVT AQSIGDQQTR
     ENANYQRENG VDEQQHTENL TKNLHNDKTI SEENHRKTDD LNKDQLKDDK NSSLNNKNIQ
     RDTTKNNNAN PSDVNQGLEQ AINDGKQSKV ASQQQSKEVD NSQDSNANNN LPSQSLTKEA
     PSLNKSDQTS QREIVNETEI EKVQPQQNNQ ANDKITNHNF NNEQEVKPQK DEKTLSVSDL
     KNNQKSPVEP TKDNDKKNGL NLLKSSAVAT LPNKGTKELT AKAKDDQTNK VAKQGQYKNQ
     DPIVLVHGFN GFTDDINPSV LAHYWGGNKM NIRQDLEENG YKAYEASISA FGSNYDRAVE
     LYYYIKGGRV DYGAAHAAKY GHERYGKTYE GIYKDWKPGQ KVHLVGHSMG GQTIRQLEEL
     LRNGNREEIE YQKKHGGEIS PLFKGNNDNM ISSITTLGTP HNGTHASDLA GNEALVRQIV
     FDIGKMFGNK NSRVDFGLAQ WGLKQKPNES YIDYVKRVKQ SNLWKSKDNG FYDLTREGAT
     DLNRKTSLNP NIVYKTYTGE ATHKALNSDR QKADLNMFFP FVITGNLIGK ATEKEWREND
     GLVSVISSQH PFNQAYTNAT DKIQKGIWQV TPTKHDWDHV DFVGQDSSDT VRTREELQDF
     WHHLADDLVK TEKVTDTKQA