ID   LIP_STAEP               Reviewed;         688 AA.
AC   P0C0R3; Q02510;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Lipase;
DE            EC=3.1.1.3;
DE   AltName: Full=Glycerol ester hydrolase;
DE   Flags: Precursor;
GN   Name=lip; Synonyms=gehC;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 303-315.
RC   STRAIN=9;
RX   PubMed=8436947; DOI=10.1099/00221287-139-2-267;
RA   Farrell A.M., Foster T.J., Holland K.T.;
RT   "Molecular analysis and expression of the lipase of Staphylococcus
RT   epidermidis.";
RL   J. Gen. Microbiol. 139:267-277(1993).
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   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M95577; AAA19729.1; -; Unassigned_DNA.
DR   PIR; A47705; A47705.
DR   RefSeq; WP_002505851.1; NZ_WJUN01000004.1.
DR   AlphaFoldDB; P0C0R3; -.
DR   SMR; P0C0R3; -.
DR   ESTHER; staep-lipas; Bacterial_lip_FamI.6.
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..35
FT                   /evidence="ECO:0000255"
FT   PROPEP          36..302
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:8436947"
FT                   /id="PRO_0000017756"
FT   CHAIN           303..688
FT                   /note="Lipase"
FT                   /id="PRO_0000017757"
FT   REGION          31..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        609
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        648
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         647
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         650
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"
FT   BINDING         658
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   688 AA;  77198 MW;  70A92F25834B9E31 CRC64;
     MKTRQNKYSI RKFSVGASSI LIAALLFMGG GSAQAAEQQQ DKGTVENSTT QSIGDGNEKL
     SEQQSTQNKN VNEKSNVNSI TENESLHNET PKNEDLIQQQ KDSQNDNKSE SVVEQNKENG
     AFVQNHSEEK PQQEQVELEK HASENNQTLH SKAAQSNEDV KTKPSQLDNT AAKQEDSQKE
     NLSKQDTQSS KTTDLLRATA QNQSKDSQST EEINKEVNND TQQVTAKNDD AKVESFNLNS
     KEEPLKVDKQ ANPTTDKDKS SKNDKGSQDG LANLESNAVA TTNKQSKQQV SEKNEDQTNK
     SAKQKQYKNN DPIILVHGFN GFTDDINPSV LTHYWGGDKM NIRQDLEENG YEAYEASISA
     FGSNYDRAVE LYYYIKGGRV DYGAAHAAKY GHERYGKTYE GVYKDWKPGQ KIHLVGHSMG
     GQTIRQLEEL LRHGNPEEVE YQKQHGGEIS PLYQGGHDNM VSSITTLGTP HNGTHASDLL
     GNEAIVRQLA YDVGKMYGNK DSRVDFGLEH WGLKQKPNES YIQYVKRVQN SKLWKSKDSG
     LHDLTRDGAT DLNRKTSLNP NIVYKTYTGE STHKTLAGKQ KADLNMFLPF TITGNLIGKA
     KEKEWRENDG LVSVISSQHP FNQKYVEATD KNQKGVWQVT PTKHDWDHVD FVGQDSTDTK
     RTRDELQQFW HGLAEDLVQS EQLTSTNK