LIP2_STAAC
ID LIP2_STAAC Reviewed; 690 AA.
AC Q5HJ48; Q5HIX5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=SACOL0317/SACOL0390;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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}.
CC -!- CAUTION: In strain COL, lip2 is interrupted in position 645 by the
CC insertion of the L54a prophage. {ECO:0000305}.
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DR EMBL; CP000046; AAW37524.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000046; AAW38859.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q5HJ48; -.
DR SMR; Q5HJ48; -.
DR ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR EnsemblBacteria; AAW37524; AAW37524; SACOL0317.
DR EnsemblBacteria; AAW38859; AAW38859; SACOL0390.
DR KEGG; sac:SACOL0317; -.
DR KEGG; sac:SACOL0390; -.
DR HOGENOM; CLU_023555_2_0_9; -.
DR Proteomes; UP000000530; 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..295
FT /evidence="ECO:0000250"
FT /id="PRO_0000045186"
FT CHAIN 296..690
FT /note="Lipase 2"
FT /id="PRO_0000045187"
FT REGION 52..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..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; 76388 MW; 8E8E3654D0E01A3B CRC64;
MLRGQEERKY SIRKYSIGVV SVLAATMFVV SSHEAQASEK TSTNAAAQKE TLNQPGEQGN
AITSHQMQSG KQLDDMHKEN GKSGTVTEGK DTLQSSKHQS TQNSKTIRTQ NDNQVKQDSE
RQGSKQSHQN NATNNTERQN DQVQNTHHAE RNGSQSTTSQ SNDVDKSQPS IPAQKVIPNH
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 FFLMATTSRI IGHDAREEWR
KNDGVVPVIS SLHPSNQPFV NVTNDEPATR RGIWQVKPII QGWDHVDFIG VDFLDFKRKG
AELANFYTGI INDLLRVEAT ESKGTQLKAS
