LIP_STAEQ
ID LIP_STAEQ Reviewed; 688 AA.
AC Q5HKP6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Glycerol ester hydrolase;
DE Flags: Precursor;
GN Name=lip; OrderedLocusNames=SERP2297;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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}.
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DR EMBL; CP000029; AAW53186.1; -; Genomic_DNA.
DR RefSeq; WP_002497700.1; NC_002976.3.
DR AlphaFoldDB; Q5HKP6; -.
DR SMR; Q5HKP6; -.
DR STRING; 176279.SERP2297; -.
DR ESTHER; staep-lipas; Bacterial_lip_FamI.6.
DR EnsemblBacteria; AAW53186; AAW53186; SERP2297.
DR KEGG; ser:SERP2297; -.
DR eggNOG; COG1075; Bacteria.
DR HOGENOM; CLU_023555_2_1_9; -.
DR OMA; NGYEAYE; -.
DR OrthoDB; 1573721at2; -.
DR Proteomes; UP000000531; 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 Reference proteome; 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_0000045196"
FT CHAIN 303..688
FT /note="Lipase"
FT /id="PRO_0000045197"
FT REGION 31..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..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; 77410 MW; 18EE607D54B0908F CRC64;
MKTRQNKYSI RKFSVGASSI LIAALLFMGG GSAQAAEQQQ DKGTVENSTT QSIGDENEKL
SEQQSTQNKN VNEKSNVDSI TENESLHNET PKNEDLIQQQ KDSQNDNKSE SVVEQNKENE
AFVKKHSEEK PQQEQVELEK HASENNQTLH SKAAQSNEDV KTKPSQLDNT TAQQEDSQKE
NLSKQDTQSS KTTDLLRATG QNQSKDSQST EEVNKEVKND TQQVTAKNDD DKVETFNLNS
KEEPLKVDKQ ANPTTDKDKS SKNDKGSHDG LANLESNAVA TTNKQSKQQV SEKNEDQTNK
SAKQKQYKNN DPIILVHGFN GFTDDINPSV LTHYWGGDKM NIRQDLEENG YEAYEASISA
FGSNYDRAVE LYYYIKGGRV DYGAAHAAKY GHERYGKTYE GVYKDWKPGQ KIHLVGHSMG
GQTIRQLEEL LRHGNPEEVE YQKQHGGEIS PLFQGGHDNM VSSITTLGTP HNGTHASDLL
GNEAIVRQLA YDVGKMYGNK DSRVDFGLEH WGLKQKPNES YIQYVKRVQN SKLWKSKDSG
LHDLTRDGAT DLNRKTSLNP NIVYKTYTGE STHKTLAGKQ KADLNMFLPF TITGNLIGKA
KEKEWRENDG LVSVISSQHP FNQKYVEATD KNQKGVWQVT PTKHDWDHVD FVGQDSTDTK
RTRDELQQFW HGLADDLVQS EQLTSTNK
