LIP1_STAAR
ID LIP1_STAAR Reviewed; 680 AA.
AC Q6GDD3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 100.
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=SAR2753;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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=CAG41728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX571856; CAG41728.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000842033.1; NC_002952.2.
DR AlphaFoldDB; Q6GDD3; -.
DR SMR; Q6GDD3; -.
DR ESTHER; staau-LIP; Bacterial_lip_FamI.6.
DR KEGG; sar:SAR2753; -.
DR HOGENOM; CLU_023555_2_1_9; -.
DR OMA; NGYEAYE; -.
DR Proteomes; UP000000596; 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_0000045180"
FT CHAIN 291..680
FT /note="Lipase 1"
FT /id="PRO_0000045181"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..260
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..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..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; 76601 MW; 4D7AB17A5A15384A CRC64;
MKSQNKYSIR KFSVGASSIL IATLLFLSGG QAQAAEKQVN MGNSQEDTVT AQSIGDQQTR
ENANYQRENG VDEQQHTENL TKNLHNDKTI SEENHRKTDD LNKDQLKDDK KSSLNNKNIQ
RDTTKNNNAN PRDVNQGLEQ AINDGKQSKV ASQQQSKEAD NSQDLNANNN LPSQSRTKVS
PSLNKSDQTS QREIVNETEI EKVQPQQKNQ ANDKITDHNF NNEQEVKPQK DEKTLSVSDL
KNNQKSPVEP TKDNDKKNGL NLLKSSAVAT LPNKGTKELT AKAKGDQTNK VAKQGQYKNQ
DPIVLVHGFN GFTDDINPSV LAHYWGGNKM NIRQDLEENG YKAYEASISA FGSNYDRAVE
LYYYIKGGRV DYGAAHAAKY GHERYGKTYE GIYKDWKPGQ KVHLVGHSMG GQTIRQLEEL
LRNGSREEIE YQKKHSGEIS PLFKGNNDNM ISSITTLGTP HNGTHASDLA GNEALVRQIV
FDIGKMFGNK NSRVDFGLAQ WGLKQKPNES YIDYVKRVKQ SNLWKSKDNG FYDLTREGAT
DLNRKTSLNP NIVYKTYTGE ATHKALNSDR QKADLNMFFP FVITGNLIGK ATEKEWREND
GLVSVISSQH PFNQAYTNAT DKIQKGIWQV TPTKHDWDHV DFVGQDSSDT VRTREELQDF
WHHLADDLVK TEKVTDTKQA
