LIP2_STAAR
ID LIP2_STAAR Reviewed; 691 AA.
AC Q6GJZ6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SAR0317;
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}.
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DR EMBL; BX571856; CAG39341.1; -; Genomic_DNA.
DR RefSeq; WP_000943842.1; NC_002952.2.
DR AlphaFoldDB; Q6GJZ6; -.
DR SMR; Q6GJZ6; -.
DR ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR KEGG; sar:SAR0317; -.
DR HOGENOM; CLU_023555_2_0_9; -.
DR OMA; DNMVASI; -.
DR OrthoDB; 1573721at2; -.
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..37
FT /evidence="ECO:0000255"
FT PROPEP 38..296
FT /evidence="ECO:0000250"
FT /id="PRO_0000045192"
FT CHAIN 297..691
FT /note="Lipase 2"
FT /id="PRO_0000045193"
FT REGION 34..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 604
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 646
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 691 AA; 76691 MW; 004B27884B347E62 CRC64;
MLRGQEERKY SIRKYSIGVV SVLAATMFVV TSHEAQASEK IPTTNAAAQK ETLNQPGEQG
NAITSHQMQS GKQLDDMHKE NGKSGTVTEG KDMLQSSKHQ STQNSKIIRT QNDNQVKQDS
ERQGSKQSHQ NNATNKTERQ NDQIQNTHHA ERNGSQSTTS QSNDVDKSQP SIPAQKVIPN
HDKAAPTSTT PPSNDKTAPK STKEQDATTD KHPNQQDTHQ PAHQIIDAKQ DDNVHQSNQK
PQVGDLSKHI DGQNSPEKPT DKNTDNKQLI KDALQAPKTR STTNAAADAK KVRPLKANQV
QPLNKYPVVF VHGFLGLVGD NAPALYPNYW GGNKYKVIEE LRKQGYNVHQ ASVSAFGSNY
DRAVELYYYI KGGRVDYGAA HAAKYGHERY GKTYKGIMPN WEPGKKVHLV GHSMGGQTIR
LMEEFLRNGN KEEIAYHKAH GGEISPLFTG GHNNMVASIT TLATPHNGSQ AADKFGNTEA
VRKIMFALNR FMGNKYSNID LGLTQWGFKQ LPNESYIDYI KRVSKSKIWT SDDNAAYDLT
LNGSAKLNNM TSMNPNITYT TYTGVSSHTG PLGYENPDLG TFFLMDTTSR IIGHDAREEW
RKNDGVVPVI SSLHPSNQPF VNVTNDEPAT RRGIWQVKPI IQGWDHVDFI GVDFLDFKRK
GAELANFYTG IINDLLRVEA TESKGTQLKA S
