LIP_STAES
ID LIP_STAES Reviewed; 688 AA.
AC P0C0R4; Q02510;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Glycerol ester hydrolase;
DE Flags: Precursor;
GN Name=lip; OrderedLocusNames=SE_0281;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO03878.1; -; Genomic_DNA.
DR RefSeq; NP_763836.1; NC_004461.1.
DR RefSeq; WP_002437845.1; NZ_WBME01000037.1.
DR AlphaFoldDB; P0C0R4; -.
DR SMR; P0C0R4; -.
DR STRING; 176280.SE_0281; -.
DR ESTHER; staep-lipas; Bacterial_lip_FamI.6.
DR EnsemblBacteria; AAO03878; AAO03878; SE_0281.
DR KEGG; sep:SE_0281; -.
DR PATRIC; fig|176280.10.peg.257; -.
DR eggNOG; COG1075; Bacteria.
DR HOGENOM; CLU_023555_2_1_9; -.
DR OMA; NGYEAYE; -.
DR Proteomes; UP000001411; 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..35
FT /evidence="ECO:0000255"
FT PROPEP 36..302
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042994"
FT CHAIN 303..688
FT /note="Lipase"
FT /id="PRO_0000042995"
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..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; 77343 MW; 6C95DB3A78AF86F6 CRC64;
MKTRQNKYSI RKFSVGASSI LIAALLFMGG GSAQAAEQQQ DKGTVENSTT QSIGDGNEKL
SEQQSTQNKN VNEKSNVNSI TENESLHNET PKNEDWIQQQ KDSQNDNKSE SVVEQNKENE
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
