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 02-SEP-2026, entry version 104. 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; Bacillati; Bacillota; Bacilli; Caryophanales; 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}. 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; 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 AbasyAtlas; Q6GCF1; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR056304; Lip-like_C. DR InterPro; IPR005877; YSIRK_signal_dom. DR NCBIfam; NF047351; lipase_YSIRK_Sa; 1. DR NCBIfam; TIGR01168; YSIRK_signal; 1. DR PANTHER; PTHR34043; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1. DR PANTHER; PTHR34043:SF3; ALPHA_BETA-HYDROLASES SUPERFAMILY PROTEIN; 1. DR Pfam; PF24708; Lip_C; 1. DR Pfam; PF04650; YSIRK_signal; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..71 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..81 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..114 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..171 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 185..206 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..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 //