LIP_STAHY
ID LIP_STAHY Reviewed; 641 AA.
AC P04635;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE EC=3.1.1.32;
DE AltName: Full=Phospholipase A1;
DE AltName: Full=Triacylglycerol lipase;
DE Contains:
DE RecName: Full=Lipase 86 kDa form;
DE Contains:
DE RecName: Full=Lipase 46 kDa form;
DE Flags: Precursor;
GN Name=lip;
OS Staphylococcus hyicus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1284;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2994017; DOI=10.1093/nar/13.16.5895;
RA Goetz F., Popp F., Korn E., Schleifer K.H.;
RT "Complete nucleotide sequence of the lipase gene from Staphylococcus hyicus
RT cloned in Staphylococcus carnosus.";
RL Nucleic Acids Res. 13:5895-5906(1985).
RN [2]
RP PROTEIN SEQUENCE OF 39-48 AND 246-251, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2611229; DOI=10.1021/bi00450a007;
RA van Oort M.G., Deveer A.M.T.J., Dijkman R., Tjeenk M.L., Verheij H.M.,
RA de Haas G.H., Wenzig E., Gotz F.;
RT "Purification and substrate specificity of Staphylococcus hyicus lipase.";
RL Biochemistry 28:9278-9285(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 222-641 IN COMPLEX WITH CALCIUM,
RP AND ACTIVE SITES.
RX PubMed=17582438; DOI=10.1016/j.jmb.2007.05.041;
RA Tiesinga J.J., van Pouderoyen G., Nardini M., Ransac S., Dijkstra B.W.;
RT "Structural basis of phospholipase activity of Staphylococcus hyicus
RT lipase.";
RL J. Mol. Biol. 371:447-456(2007).
CC -!- FUNCTION: Has a broad substrate specificity hydrolyzing a variety of
CC triglycerides and phosphatidylcholines. {ECO:0000269|PubMed:2611229}.
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 Evidence={ECO:0000269|PubMed:2611229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:2611229};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:2611229};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH around 9. {ECO:0000269|PubMed:2611229};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2611229}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X02844; CAA26602.1; -; Genomic_DNA.
DR PIR; A24075; A24075.
DR PDB; 2HIH; X-ray; 2.86 A; A/B=222-641.
DR PDBsum; 2HIH; -.
DR AlphaFoldDB; P04635; -.
DR SMR; P04635; -.
DR STRING; 1284.SHYC_01855; -.
DR ESTHER; stahy-lipas; Bacterial_lip_FamI.6.
DR EvolutionaryTrace; P04635; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:2611229"
FT CHAIN 39..641
FT /note="Lipase 86 kDa form"
FT /id="PRO_0000017758"
FT CHAIN 246..641
FT /note="Lipase 46 kDa form"
FT /id="PRO_0000017759"
FT REGION 41..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17582438"
FT ACT_SITE 559
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:17582438"
FT ACT_SITE 600
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:17582438"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17582438"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17582438"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17582438"
FT BINDING 607
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17582438"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17582438"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2HIH"
FT TURN 285..290
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:2HIH"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 435..450
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 541..547
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 564..568
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2HIH"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:2HIH"
FT HELIX 615..637
FT /evidence="ECO:0007829|PDB:2HIH"
SQ SEQUENCE 641 AA; 71224 MW; 8C73DC4DCC8CEE07 CRC64;
MKETKHQHTF SIRKSAYGAA SVMVASCIFV IGGGVAEAND STTQTTTPLE VAQTSQQETH
THQTPVTSLH TATPEHVDDS KEATPLPEKA ESPKTEVTVQ PSSHTQEVPA LHKKTQQQPA
YKDKTVPEST IASKSVESNK ATENEMSPVE HHASNVEKRE DRLETNETTP PSVDREFSHK
IINNTHVNPK TDGQTNVNVD TKTIDTVSPK DDRIDTAQPK QVDVPKENTT AQNKFTSQAS
DKKPTVKAAP EAVQNPENPK NKDPFVFVHG FTGFVGEVAA KGENHWGGTK ANLRNHLRKA
GYETYEASVS ALASNHERAV ELYYYLKGGR VDYGAAHSEK YGHERYGKTY EGVLKDWKPG
HPVHFIGHSM GGQTIRLLEH YLRFGDKAEI AYQQQHGGII SELFKGGQDN MVTSITTIAT
PHNGTHASDD IGNTPTIRNI LYSFAQMSSH LGTIDFGMDH WGFKRKDGES LTDYNKRIAE
SKIWDSEDTG LYDLTREGAE KINQKTELNP NIYYKTYTGV ATHETQLGKH IADLGMEFTK
ILTGNYIGSV DDILWRPNDG LVSEISSQHP SDEKNISVDE NSELHKGTWQ VMPTMKGWDH
SDFIGNDALD TKHSAIELTN FYHSISDYLM RIEKAESTKN A
