ID   LIFO_BURVG              Reviewed;         344 AA.
AC   A4JM56;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Lipase chaperone {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase activator protein {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase foldase {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase helper protein {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase modulator {ECO:0000255|HAMAP-Rule:MF_00790};
GN   Name=lifO {ECO:0000255|HAMAP-Rule:MF_00790};
GN   OrderedLocusNames=Bcep1808_4393;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the folding of the extracellular lipase
CC       during its passage through the periplasm. {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00790}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00790}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
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DR   EMBL; CP000615; ABO57359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JM56; -.
DR   SMR; A4JM56; -.
DR   STRING; 269482.Bcep1808_4393; -.
DR   EnsemblBacteria; ABO57359; ABO57359; Bcep1808_4393.
DR   KEGG; bvi:Bcep1808_4393; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_064928_1_0_4; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000002287; Chromosome 2.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Lipid degradation;
KW   Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..344
FT                   /note="Lipase chaperone"
FT                   /id="PRO_1000046915"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ   SEQUENCE   344 AA;  36567 MW;  32C429D61C3DB75C CRC64;
     MSAQQTRAPL LRRIAPYGAA GLAAIVGVAI WSGTGSQSGA DASRTPANAV AADGASAAVR
     QAALPASAAL PAPLVGSSAP RLPLDSGGHL AKVRAVRDFF DYCLTARSEL TAAALDALVA
     REIAAQLDAT PAQPEALDVW RRYRAYLDAL EKLPDGGAVD KIDPEALQRA LDQRASIAHR
     TLGDWSQPFF GAEQSQQRYD LARLRIVQDR TLTDAQKAER LAALDQQMPA DERAARAPAE
     RQRAALDQIA QLQKSGATPD AVRAQLTQSL GADVAARVVQ MQQDDASWQS RYADYAAQRA
     QIDAAGLSQQ DRDAQIAALR QRIFTKPGEA VRAAAFDRSA AGTR