LIP2_STAAS
ID LIP2_STAAS Reviewed; 690 AA.
AC Q6GCF1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Lipase 2;
DE EC=3.1.1.3;
DE AltName: Full=Glycerol ester hydrolase 2;
DE Flags: Precursor;
GN Name=lip2; Synonyms=geh; OrderedLocusNames=SAS0297;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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}.
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DR EMBL; BX571857; CAG42068.1; -; Genomic_DNA.
DR RefSeq; WP_000943814.1; NC_002953.3.
DR AlphaFoldDB; Q6GCF1; -.
DR SMR; Q6GCF1; -.
DR ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR KEGG; sas:SAS0297; -.
DR HOGENOM; CLU_023555_2_0_9; -.
DR OMA; DNMVASI; -.
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..37
FT /evidence="ECO:0000255"
FT PROPEP 38..295
FT /evidence="ECO:0000250"
FT /id="PRO_0000045194"
FT CHAIN 296..690
FT /note="Lipase 2"
FT /id="PRO_0000045195"
FT REGION 53..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 603
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 645
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 652
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"
SQ SEQUENCE 690 AA; 76522 MW; 36FFB5E0BB434CCA CRC64;
MLRGQEERKY SIRKYSIGVV SVLAATMFVV SSHEAQASEK TPTNAAVQKE TLNQPGEQGN
AITSHQMQSG KQLDDMHKEN GKSGTVTEGK DTLQLSKYQS TQNSKTIRTQ NDNQVKQDSE
RQGSKQSHQN NATNNTERQN DQVQNTHHAE RNGSQSTTSQ SNDVDKSQPS IPAQKVLPNH
DKAAPTSTTP PSNDKTAPKS TKAQDATTDK HPNQQDTHQP AHQIIDAKQD DTVRQSEQKP
QVGDLSKHID GQNSPEKPTD KNTDNKQLIK DALQAPKTRS TTNAAADAKK VRPLKANQVQ
PLNKYPVVFV HGFLGLVGDN APALYPNYWG GNKFKVIEEL RKQGYNVHQA SVSAFGSNYD
RAVELYYYIK GGRVDYGAAH AAKYGHERYG KTYKGIMPNW EPGKKVHLVG HSMGGQTIRL
MEEFLRNGNK EEIAYHKAHG GEISPLFTGG HNNMVASITT LATPHNGSQA ADKFGNTEAV
RKIMFALNRF MGNKYSNIDL GLTQWGFKQL PNESYIDYIK RVSKSKIWTS DDNAAYDLTL
DGSAKLNNMT SMNPNITYTT YTGVSSHTGP LGYENPDLGT FFLMDTTSRI IGHDAREEWR
KNDGVVPVIS SLHPSNQPFV NVTNDEPATR RGIWQVKPII QGWDHVDFIG VDFLDFKRKG
AELANFYTGI INDLLRVEAT ESKGTQLKAS
