LIP_BACSP
ID LIP_BACSP Reviewed; 416 AA.
AC Q5U780;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 3.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Lip 42;
DE AltName: Full=Thermostable organic solvent tolerant lipase;
DE AltName: Full=Triacylglycerol hydrolase;
DE Flags: Precursor;
OS Bacillus sp.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1409;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SOLVENT STABILITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=42;
RX DOI=10.1007/BF03175607;
RA Hamid T.H.T.A., Eltaweel M.A., Rahman R.N.Z.R.A., Basri M., Salleh A.B.;
RT "Characterization and solvent stable features of Strep-tagged purified
RT recombinant lipase from thermostable and solvent tolerant Bacillus sp.
RT strain 42.";
RL Ann. Microbiol. 59:111-118(2009).
RN [2]
RP SEQUENCE REVISION TO 175.
RA Khusaini M.S., Rahman R.N.Z.R.A.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 29-416 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, AND ACTIVE SITES.
RC STRAIN=42;
RA Zaliha R.N., Rahman R.A., Khusaini M.S.;
RT "An Organic solvent tolerant lipase 42.";
RL Submitted (JUN-2012) to the PDB data bank.
CC -!- FUNCTION: Triacylglycerol hydrolase that shows hydrolysis preference
CC towards some of the natural oils such as olive, sunflower and corn
CC oils. {ECO:0000269|Ref.1}.
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|Ref.1};
CC -!- ACTIVITY REGULATION: Activity is inhibited by zinc and iron ions, and
CC activated in vitro in 25% v/v DMSO and acetone. {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. Is stable in a broad pH range of 7-10.
CC {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Highly thermostable with a
CC half-life of 315 minutes at 60 degrees Celsius, 125 minutes at 65
CC degrees Celsius and 45 minutes at 70 degrees Celsius.
CC {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: Is stable in polar organic solvents such as DMSO, DMF,
CC acetone, methanol, ethanol, heptanol and octanol, which could make it
CC as a potential biocatalyst for the use in industrial biodiesel
CC production.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AY787835; AAV35102.2; -; Genomic_DNA.
DR PDB; 4FKB; X-ray; 1.22 A; A/B=29-416.
DR PDBsum; 4FKB; -.
DR AlphaFoldDB; Q5U780; -.
DR SMR; Q5U780; -.
DR ESTHER; bacsp-lip; Bacterial_lip_FamI.5.
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 SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..416
FT /note="Lipase"
FT /id="PRO_0000419954"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000269|Ref.3"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000269|Ref.3"
FT ACT_SITE 386
FT /note="Charge relay system"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4FKB"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4FKB"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:4FKB"
FT TURN 386..391
FT /evidence="ECO:0007829|PDB:4FKB"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:4FKB"
SQ SEQUENCE 416 AA; 46353 MW; 83E9005EDC6729BE CRC64;
MKCCRIMFVL LGLWFVFGLS VPGGRTEAAS LRANDAPIVL LHGFTGWGRE EMFGFKYWGG
VRGDIEQWLN DNGYRTYTLA VGPLSSNWDR ACEAYAQLVG GTVDYGAAHA AKHGHARFGR
TYPGLLPELK RGGRIHIIAH SQGGQTARML VSLLENGSQE EREYAKAHNV SLSPLFEGGH
HFVLSVTTIA TPHDGTTLVN MVDFTDRFFD LQKAVLEAAA VASNVPYTSQ VYDFKLDQWG
LRRQPGESFD HYFERLKRSP VWTSTDTARY DLSVSGAEKL NQWVQASPNT YYLSFSTERT
YRGALTGNHY PELGMNAFSA VVCAPFLGSY RNPTLGIDDR WLENDGIVNT VSMNGPKRGS
SDRIVPYDGT LKKGVWNDMG TYNVDHLEII GVDPNPSFDI RAFYLRLAEQ LASLRP
