LIP_BURPL
ID LIP_BURPL Reviewed; 358 AA.
AC P0DUB8; Q05489;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:1476423};
DE EC=3.1.1.3 {ECO:0000305|PubMed:1476423};
DE AltName: Full=Extracellular lipase {ECO:0000303|PubMed:1476423};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
DE Flags: Precursor;
GN Name=lip {ECO:0000305}; Synonyms=lipA {ECO:0000303|PubMed:1476423};
OS Burkholderia plantarii.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=41899;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-61, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-54;
RP SER-126; ASP-160; ASP-280; ASP-302 AND HIS-324, SUBCELLULAR LOCATION,
RP ACTIVE SITE, AND NOMENCLATURE.
RC STRAIN=PG1 / CBS 322.89;
RX PubMed=1476423; DOI=10.1128/aem.58.12.3787-3791.1992;
RA Frenken L.G.J., Egmond M.R., Batenburg A.M., Bos J.W., Visser C.,
RA Verrips C.T.;
RT "Cloning of the Pseudomonas glumae lipase gene and determination of the
RT active site residues.";
RL Appl. Environ. Microbiol. 58:3787-3791(1992).
RN [2]
RP PROTEIN SEQUENCE OF 40-54, AND FUNCTION.
RX PubMed=7786905; DOI=10.1016/0005-2760(95)00052-e;
RA Taipa M.A., Liebeton K., Costa J.V., Cabral J.M.S., Jaeger K.-E.;
RT "Lipase from Chromobacterium viscosum: biochemical characterization
RT indicating homology to the lipase from Pseudomonas glumae.";
RL Biochim. Biophys. Acta 1256:396-402(1995).
RN [3]
RP SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=PG1 / CBS 322.89;
RX PubMed=8412704; DOI=10.1111/j.1365-2958.1993.tb01718.x;
RA Frenken L.G.J., Bos J.W., Visser C., Mueller W., Tommassen J.,
RA Verrips C.T.;
RT "An accessory gene, lipB, required for the production of active Pseudomonas
RT glumae lipase.";
RL Mol. Microbiol. 9:579-589(1993).
RN [4]
RP FOLDING AND ASSEMBLY.
RC STRAIN=PG1 / CBS 322.89;
RX PubMed=8412705; DOI=10.1111/j.1365-2958.1993.tb01719.x;
RA Frenken L.G.J., de Groot A., Tommassen J., Verrips C.T.;
RT "Role of the lipB gene product in the folding of the secreted lipase of
RT Pseudomonas glumae.";
RL Mol. Microbiol. 9:591-599(1993).
RN [5] {ECO:0007744|PDB:1TAH}
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 41-358 IN COMPLEX WITH CALCIUM
RP ION, COFACTOR, ACTIVE SITE, DISULFIDE BOND, AND SUBUNIT.
RC STRAIN=PG1 / CBS 322.89;
RX PubMed=8405390; DOI=10.1016/0014-5793(93)80310-q;
RA Noble M.E.M., Cleasby A., Johnson L.N., Egmond M.R., Frenken L.G.J.;
RT "The crystal structure of triacylglycerol lipase from Pseudomonas glumae
RT reveals a partially redundant catalytic aspartate.";
RL FEBS Lett. 331:123-128(1993).
RN [6] {ECO:0007744|PDB:2ES4}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 40-358 IN COMPLEX WITH LIFO AND
RP CALCIUM ION, COFACTOR, DISULFIDE BOND, AND SUBUNIT.
RC STRAIN=PG1 / CBS 322.89;
RX PubMed=16518399; DOI=10.1038/nsmb1065;
RA Pauwels K., Lustig A., Wyns L., Tommassen J., Savvides S.N., Van Gelder P.;
RT "Structure of a membrane-based steric chaperone in complex with its lipase
RT substrate.";
RL Nat. Struct. Mol. Biol. 13:374-375(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol.
CC {ECO:0000269|PubMed:1476423, ECO:0000269|PubMed:7786905}.
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:0000305|PubMed:1476423};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:16518399,
CC ECO:0000269|PubMed:8405390};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for oil emulsion {ECO:0000269|PubMed:1476423};
CC Vmax=4 umol/min/mg enzyme {ECO:0000269|PubMed:1476423};
CC -!- SUBUNIT: Monomer (Probable). Interacts with lipase-specific foldase Lif
CC (PubMed:16518399). {ECO:0000269|PubMed:16518399,
CC ECO:0000305|PubMed:16518399, ECO:0000305|PubMed:8405390}.
CC -!- INTERACTION:
CC P0DUB8; Q05490: lifO; NbExp=3; IntAct=EBI-26563962, EBI-993746;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:1476423,
CC ECO:0000305|PubMed:8412704}. Note=Correct periplasmic folding,
CC necessary for secretion, requires the lipase-specific foldase LifO
CC (also called lipB). Secretion probably occurs via a type II secretion
CC system. {ECO:0000269|PubMed:8412705, ECO:0000305|PubMed:8412704}.
CC -!- INDUCTION: By growth on olive oil or oleic acid; part of the lip-lifO
CC (also called lipA-lipB) operon. {ECO:0000269|PubMed:8412704}.
CC -!- DISRUPTION PHENOTYPE: Loss of extracellular active lipase. Not required
CC for growth on oleic acid as a carbon source.
CC {ECO:0000269|PubMed:8412704}.
CC -!- BIOTECHNOLOGY: Found to be superior in improving overall detergency.
CC {ECO:0000269|PubMed:8412704}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
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DR EMBL; X70354; CAA49812.1; -; Genomic_DNA.
DR PIR; A48952; A48952.
DR RefSeq; WP_042628289.1; NZ_CP007213.1.
DR PDB; 1TAH; X-ray; 3.00 A; A/B/C/D=41-358.
DR PDB; 2ES4; X-ray; 1.85 A; A/B=40-358.
DR PDBsum; 1TAH; -.
DR PDBsum; 2ES4; -.
DR AlphaFoldDB; P0DUB8; -.
DR SMR; P0DUB8; -.
DR DIP; DIP-29069N; -.
DR IntAct; P0DUB8; 1.
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; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:1476423"
FT CHAIN 40..358
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000017741"
FT DOMAIN 48..327
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:1476423,
FT ECO:0000305|PubMed:8405390"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:1476423,
FT ECO:0000305|PubMed:8405390"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:1476423,
FT ECO:0000305|PubMed:8405390"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16518399,
FT ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH,
FT ECO:0007744|PDB:2ES4"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16518399,
FT ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH,
FT ECO:0007744|PDB:2ES4"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16518399,
FT ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH,
FT ECO:0007744|PDB:2ES4"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16518399,
FT ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH,
FT ECO:0007744|PDB:2ES4"
FT DISULFID 229..308
FT /evidence="ECO:0000269|PubMed:16518399,
FT ECO:0000269|PubMed:8405390"
FT MUTAGEN 54
FT /note="H->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 126
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 160
FT /note="D->A,E: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 280
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 280
FT /note="D->E: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 302
FT /note="D->A: 75% loss of activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 302
FT /note="D->E: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT MUTAGEN 324
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1476423"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2ES4"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:2ES4"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2ES4"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1TAH"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:2ES4"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:2ES4"
FT TURN 329..333
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:2ES4"
SQ SEQUENCE 358 AA; 36929 MW; FE7B5D7A22EC6B4B CRC64;
MVRSMRSRVA ARAVAWALAV MPLAGAAGLT MAASPAAVAA DTYAATRYPV ILVHGLAGTD
KFANVVDYWY GIQSDLQSHG AKVYVANLSG FQSDDGPNGR GEQLLAYVKQ VLAATGATKV
NLIGHSQGGL TSRYVAAVAP QLVASVTTIG TPHRGSEFAD FVQDVLKTDP TGLSSTVIAA
FVNVFGTLVS SSHNTDQDAL AALRTLTTAQ TATYNRNFPS AGLGAPGSCQ TGAATETVGG
SQHLLYSWGG TAIQPTSTVL GVTGATDTST GTLDVANVTD PSTLALLATG AVMINRASGQ
NDGLVSRCSS LFGQVISTSY HWNHLDEINQ LLGVRGANAE DPVAVIRTHV NRLKLQGV
