ID   LIFO2_BURCE             Reviewed;         344 AA.
AC   Q9ZEM5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Lipase chaperone;
DE   AltName: Full=Lipase activator protein;
DE   AltName: Full=Lipase foldase;
DE   AltName: Full=Lipase helper protein;
DE   AltName: Full=Lipase modulator;
GN   Name=lifO; Synonyms=hp, lipB;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21808 / FERM P-1431 / 156-A;
RX   PubMed=9925617; DOI=10.1128/aem.65.2.787-794.1999;
RA   Quyen D.T., Schmidt-Dannert C., Schmid R.D.;
RT   "High-level formation of active Pseudomonas cepacia lipase after
RT   heterologous expression of the encoding gene and its modified chaperone in
RT   Escherichia coli and rapid in vitro refolding.";
RL   Appl. Environ. Microbiol. 65:787-794(1999).
CC   -!- FUNCTION: May be involved in the folding of the extracellular lipase
CC       during its passage through the periplasm.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000305}.
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DR   EMBL; AJ131766; CAA10510.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZEM5; -.
DR   SMR; Q9ZEM5; -.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..344
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218480"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   344 AA;  36422 MW;  AC37A4EF919B71B5 CRC64;
     MTAREGRAPL ARCAVVYGVV GLAAIAGVAM WSGAGWHRGT GTAGELPDAA AAGGAAAAPP
     QAALPASTGL PSSLAGSSAP RLPLDAGGHL AKSRAVRDFF DYCLTAQSDL SAAALDAFVV
     RQIAAQLDGT VAQAEALDVW HRYRAYLDAL AKLRDAGAVD KSDLGALQLA LDQRASIAYR
     TLGDWSQPFF GAEQWRQRYD LARLKIAQDR TLTDAQKAER LAALEQQMPA DERAAQQRVD
     QQRAAIDRIA QLQKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQS RYADYATQRA
     EIESAGLSPQ DRDAQIAALR QRTFTKPGEA VRAASLDRGA GSAQ