LIFO_BURPL
ID LIFO_BURPL Reviewed; 353 AA.
AC Q05490;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Lipase-specific foldase {ECO:0000303|PubMed:8412705};
DE Short=Lif {ECO:0000303|PubMed:16518399};
DE AltName: Full=Lipase activator protein;
DE AltName: Full=Lipase chaperone;
DE AltName: Full=Lipase helper protein;
DE AltName: Full=Lipase modulator;
GN Name=lifO {ECO:0000305}; Synonyms=lipB {ECO:0000303|PubMed:8412704};
OS Burkholderia plantarii.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=41899;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, DISRUPTION PHENOTYPE, AND TOPOLOGY.
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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [3] {ECO:0007744|PDB:2ES4}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 42-352 IN COMPLEX WITH LIP,
RP FUNCTION, 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: Involved in the folding of the extracellular lipase (lip)
CC during its passage through the periplasm. {ECO:0000269|PubMed:8412705,
CC ECO:0000305|PubMed:8412704}.
CC -!- SUBUNIT: Monomer. Interacts with lipase (lip).
CC {ECO:0000269|PubMed:16518399}.
CC -!- INTERACTION:
CC Q05490; P0DUB8: lip; NbExp=3; IntAct=EBI-993746, EBI-26563962;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8412704};
CC Single-pass membrane protein {ECO:0000305|PubMed:8412704}; Periplasmic
CC side {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: Significant loss of extracellular active lipase
CC (lip). Not required for growth on oleic acid as a carbon source
CC (PubMed:8412704). Cells can translate lipase; while its signal peptide
CC is processed, it is not secreted (PubMed:8412705).
CC {ECO:0000269|PubMed:8412704, ECO:0000269|PubMed:8412705}.
CC -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000305}.
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DR EMBL; X70354; CAA49813.1; -; Genomic_DNA.
DR PIR; S36249; S36249.
DR RefSeq; WP_042628288.1; NZ_CP002581.1.
DR PDB; 2ES4; X-ray; 1.85 A; D/E=42-352.
DR PDBsum; 2ES4; -.
DR AlphaFoldDB; Q05490; -.
DR SMR; Q05490; -.
DR DIP; DIP-29068N; -.
DR IntAct; Q05490; 1.
DR PRIDE; Q05490; -.
DR EvolutionaryTrace; Q05490; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00790; Lipase_chap; 1.
DR InterPro; IPR004961; Lipase_chaperone.
DR Pfam; PF03280; Lipase_chap; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone;
KW Lipid degradation; Lipid metabolism; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..353
FT /note="Lipase-specific foldase"
FT /id="PRO_0000218481"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8412704"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..353
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8412704"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:2ES4"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 197..218
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 241..265
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 283..314
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:2ES4"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:2ES4"
SQ SEQUENCE 353 AA; 36831 MW; 57C5916D78EBB643 CRC64;
MAQADRPARG GLAARPMRGA SFALAGLVAC AACAAVVLWL RPAAPSPAPA GAVAGGPAAG
VPAAASGAAE AAMPLPAALP GALAGSHAPR LPLAAGGRLA RTRAVREFFD YCLTAQGELT
PAALDALVRR EIAAQLDGSP AQAEALGVWR RYRAYFDALA QLPGDGAVLG DKLDPAAMQL
ALDQRAALAD RTLGEWAEPF FGDEQRRQRH DLERIRIAND TTLSPEQKAA RLAALDAQLT
PDERAQQAAL HAQQDAVTKI ADLQKAGATP DQMRAQIAQT LGPEAAARAA QMQQDDEAWQ
TRYQAYAAER DRIAAQGLAP QDRDARIAQL RQQTFTAPGE AIRAASLDRG AGG
