LIP_PSEAE
ID LIP_PSEAE Reviewed; 311 AA.
AC P26876;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:1748875};
DE EC=3.1.1.3 {ECO:0000305|PubMed:1748875};
DE AltName: Full=Extracellular lipase {ECO:0000303|PubMed:1748875};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000303|PubMed:1512563};
DE Flags: Precursor;
GN Name=lip {ECO:0000305}; Synonyms=lipA {ECO:0000303|PubMed:1512563};
GN OrderedLocusNames=PA2862;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1512563; DOI=10.1099/00221287-138-7-1325;
RA Wohlfarth S., Hoesche C., Strunk C., Winkler U.K.;
RT "Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa
RT PAO1.";
RL J. Gen. Microbiol. 138:1325-1335(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP ACTIVE SITE.
RC STRAIN=TE3285;
RX PubMed=1632642; DOI=10.1016/0003-9861(92)90604-u;
RA Chihara-Siomi M., Yoshikawa K., Oshima-Hirayama N., Yamamoto K., Sogabe Y.,
RA Nakatani T., Nishioka T., Oda J.;
RT "Purification, molecular cloning, and expression of lipase from Pseudomonas
RT aeruginosa.";
RL Arch. Biochem. Biophys. 296:505-513(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-57, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=PAC1R;
RX PubMed=1576157; DOI=10.1016/0167-4838(92)90254-b;
RA Jaeger K.-E., Adrian F.-J., Meyer H.E., Hancock R.E.W., Winkler U.K.;
RT "Extracellular lipase from Pseudomonas aeruginosa is an amphiphilic
RT protein.";
RL Biochim. Biophys. Acta 1120:315-321(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [5]
RP PROTEIN SEQUENCE OF 28-39, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=EF2;
RX PubMed=1748875; DOI=10.1099/00221287-137-9-2223;
RA Gilbert E.J., Cornish A., Jones C.W.;
RT "Purification and properties of extracellular lipase from Pseudomonas
RT aeruginosa EF2.";
RL J. Gen. Microbiol. 137:2223-2229(1991).
RN [6]
RP MUTAGENESIS OF CYS-209 AND CYS-261, AND DISULFIDE BOND.
RX PubMed=11133953; DOI=10.1128/jb.183.2.597-603.2001;
RA Liebeton K., Zacharias A., Jaeger K.-E.;
RT "Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure
RT but is not required for interaction with its foldase.";
RL J. Bacteriol. 183:597-603(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF COMPLEX WITH SUBSTRATE ANALOG AND
RP CALCIUM ION, ACTIVE SITE, COFACTOR, AND DISULFIDE BOND.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10893416; DOI=10.1074/jbc.m003903200;
RA Nardini M., Lang D.A., Liebeton K., Jaeger K.-E., Dijkstra B.W.;
RT "Crystal structure of Pseudomonas aeruginosa lipase in the open
RT conformation. The prototype for family I.1 of bacterial lipases.";
RL J. Biol. Chem. 275:31219-31225(2000).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol (PubMed:1748875).
CC It also exhibits some esterase activity with p-nitrophenyl acetate and
CC Tween 80 as substrates, however the lipase activity is approximately
CC eight times the esterase activity (PubMed:1748875). It shows a marked
CC specificity for the 1,3-oleyl residues of triolein (PubMed:1748875).
CC {ECO:0000269|PubMed:1748875, ECO:0000305|PubMed:1632642}.
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:1748875};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10893416};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10893416};
CC -!- ACTIVITY REGULATION: Na(+) increases lipase activity (PubMed:1748875).
CC Inhibited by diethyl p-nitrophenyl phosphate and 3,4-
CC dichloroisocoumarin (DCI) (PubMed:1576157, PubMed:1748875).
CC {ECO:0000269|PubMed:1576157, ECO:0000269|PubMed:1748875}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9. {ECO:0000269|PubMed:1748875};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:1748875};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1748875}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1576157}.
CC Note=During early stationary growth phase about 10% of the enzyme
CC molecules remain cell-bound while about 90% are released into the
CC growth medium. {ECO:0000269|PubMed:1576157}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
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DR EMBL; X63390; CAA44997.1; -; Genomic_DNA.
DR EMBL; AB008452; BAA23128.1; -; Genomic_DNA.
DR EMBL; AX000441; CAB77076.1; -; Unassigned_DNA.
DR EMBL; AE004091; AAG06250.1; -; Genomic_DNA.
DR PIR; S25768; S25768.
DR RefSeq; NP_251552.1; NC_002516.2.
DR RefSeq; WP_003090955.1; NZ_QZGE01000011.1.
DR PDB; 1EX9; X-ray; 2.54 A; A=27-311.
DR PDBsum; 1EX9; -.
DR AlphaFoldDB; P26876; -.
DR SMR; P26876; -.
DR STRING; 287.DR97_5079; -.
DR ESTHER; pseae-llipa; Bacterial_lip_FamI.1.
DR PaxDb; P26876; -.
DR DNASU; 882662; -.
DR EnsemblBacteria; AAG06250; AAG06250; PA2862.
DR GeneID; 882662; -.
DR KEGG; pae:PA2862; -.
DR PATRIC; fig|208964.12.peg.3002; -.
DR PseudoCAP; PA2862; -.
DR HOGENOM; CLU_062016_0_0_6; -.
DR InParanoid; P26876; -.
DR OMA; YYFSWSG; -.
DR PhylomeDB; P26876; -.
DR BioCyc; PAER208964:G1FZ6-2912-MON; -.
DR BRENDA; 3.1.1.3; 5087.
DR EvolutionaryTrace; P26876; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IDA:PseudoCAP.
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 GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1576157"
FT CHAIN 27..311
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000017739"
FT DOMAIN 35..280
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10893416,
FT ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10893416,
FT ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10893416,
FT ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0007744|PDB:1EX9"
FT DISULFID 209..261
FT /evidence="ECO:0000269|PubMed:10893416,
FT ECO:0000269|PubMed:11133953, ECO:0007744|PDB:1EX9"
FT VARIANT 33
FT /note="K -> Q (in strain: EF2)"
FT VARIANT 156
FT /note="V -> I (in strain: TE3285)"
FT VARIANT 202
FT /note="Q -> H (in strain: TE3285)"
FT VARIANT 204
FT /note="I -> V (in strain: TE3285)"
FT MUTAGEN 209
FT /note="C->S: Loss of lipase activity."
FT /evidence="ECO:0000269|PubMed:11133953"
FT MUTAGEN 261
FT /note="C->S: Loss of lipase activity."
FT /evidence="ECO:0000269|PubMed:11133953"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 79..97
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 152..173
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:1EX9"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:1EX9"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1EX9"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:1EX9"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:1EX9"
SQ SEQUENCE 311 AA; 32723 MW; 7DB14DF27BDE5619 CRC64;
MKKKSLLPLG LAIGLASLAA SPLIQASTYT QTKYPIVLAH GMLGFDNILG VDYWFGIPSA
LRRDGAQVYV TEVSQLDTSE VRGEQLLQQV EEIVALSGQP KVNLIGHSHG GPTIRYVAAV
RPDLIASATS VGAPHKGSDT ADFLRQIPPG SAGEAVLSGL VNSLGALISF LSSGSTGTQN
SLGSLESLNS EGAARFNAKY PQGIPTSACG EGAYKVNGVS YYSWSGSSPL TNFLDPSDAF
LGASSLTFKN GTANDGLVGT CSSHLGMVIR DNYRMNHLDE VNQVFGLTSL FETSPVSVYR
QHANRLKNAS L
