LIP_PSEPS
ID LIP_PSEPS Reviewed; 319 AA.
AC P0DUB9; Q05489;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Triacylglycerol lipase {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000305|PubMed:7786905};
DE AltName: Full=Extracellular lipase {ECO:0000305};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
GN Name=lip {ECO:0000305}; Synonyms=lipA {ECO:0000303|PubMed:7786905};
OS Pseudarthrobacter phenanthrenivorans (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=361575;
RN [1]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, AND CATALYTIC ACTIVITY.
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 [2] {ECO:0007744|PDB:1CVL}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF THE CLOSED FORM IN COMPLEX WITH
RP CALCIUM, COFACTOR, ACTIVE SITE, MASS SPECTROMETRY, DISULFIDE BOND, SUBUNIT,
RP AND BIOTECHNOLOGY.
RC STRAIN=ATCC 6918 / DSM 20144 / NCIMB 8180 / NCTC 2416;
RX PubMed=8683577; DOI=10.1006/jmbi.1996.0352;
RA Lang D., Hofmann B., Haalck L., Hecht H.-J., Spener F., Schmid R.D.,
RA Schomburg D.;
RT "Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC
RT 6918 refined at 1.6-A resolution.";
RL J. Mol. Biol. 259:704-717(1996).
RN [3] {ECO:0007744|PDB:1QGE}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 40-261 AND 262-358 IN COMPLEX
RP WITH CALCIUM ION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 6918 / DSM 20144 / NCIMB 8180 / NCTC 2416;
RA Lang D.A., Stadler P., Kovacs A., Paltauf F., Dijkstra B.W.;
RT "Structural and kinetic investigations of enantiomeric binding mode of
RT subclass I lipases from the family of Pseudomonadaceae.";
RL Submitted (APR-1999) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol.
CC {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:7786905};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8683577, ECO:0000305|Ref.3};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:8683577,
CC ECO:0000305|Ref.3};
CC -!- SUBUNIT: Monomer (Probable). Interacts with lipase-specific foldase Lif
CC (By similarity). {ECO:0000250|UniProtKB:P0DUB8,
CC ECO:0000305|PubMed:8683577, ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUB8}.
CC Note=Correct periplasmic folding, necessary for secretion, requires the
CC lipase-specific foldase LifO. Secretion probably occurs via a type II
CC secretion system. {ECO:0000250|UniProtKB:P0DUB8}.
CC -!- MASS SPECTROMETRY: Mass=32839; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8683577};
CC -!- BIOTECHNOLOGY: Found to be superior in improving overall detergency.
CC {ECO:0000269|PubMed:8683577}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {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 PDB; 1CVL; X-ray; 1.60 A; A=1-319.
DR PDB; 1QGE; X-ray; 1.70 A; D=1-222, E=223-319.
DR PDBsum; 1CVL; -.
DR PDBsum; 1QGE; -.
DR AlphaFoldDB; P0DUB9; -.
DR SMR; P0DUB9; -.
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.
FT CHAIN 1..319
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000451466"
FT DOMAIN 10..288
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:8683577"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8683577"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8683577"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8683577,
FT ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8683577,
FT ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8683577,
FT ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8683577,
FT ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"
FT DISULFID 190..269
FT /evidence="ECO:0000269|PubMed:8683577"
FT UNSURE 220..224
FT /evidence="ECO:0000305"
FT CONFLICT 1
FT /note="A -> W (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1CVL"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1QGE"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1CVL"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1CVL"
FT TURN 290..294
FT /evidence="ECO:0007829|PDB:1CVL"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:1CVL"
SQ SEQUENCE 319 AA; 33092 MW; 899526CADED66B05 CRC64;
ADTYAATRYP VILVHGLAGT DKFANVVDYW YGIQSDLQSH GAKVYVANLS GFQSDDGPNG
RGEQLLAYVK QVLAATGATK VNLIGHSQGG LTSRYVAAVA PQLVASVTTI GTPHRGSEFA
DFVQDVLKTD PTGLSSTVIA AFVNVFGTLV SSSHNTDQDA LAALRTLTTA QTATYNRNFP
SAGLGAPGSC QTGAATETVG GSQHLLYSWG GTAIQPTSTV LGVTGATDTS TGTLDVANVT
DPSTLALLAT GAVMINRASG QNDGLVSRCS SLFGQVISTS YHWNHLDEIN QLLGVRGANA
EDPVAVIRTH VNRLKLQGV
