ID   LIFO1_BURCE             Reviewed;         344 AA.
AC   P22089;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=limA, 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=DSM 3959;
RX   PubMed=1987151; DOI=10.1128/jb.173.2.559-567.1991;
RA   Joergensen S., Skov K.W., Diderichsen B.;
RT   "Cloning, sequence, and expression of a lipase gene from Pseudomonas
RT   cepacia: lipase production in heterologous hosts requires two Pseudomonas
RT   genes.";
RL   J. Bacteriol. 173:559-567(1991).
CC   -!- FUNCTION: May be involved in the folding of the extracellular lipase
CC       during its passage through the periplasm. {ECO:0000250}.
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; M58494; AAA50467.1; -; Genomic_DNA.
DR   PIR; B39133; B39133.
DR   AlphaFoldDB; P22089; -.
DR   SMR; P22089; -.
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_0000218479"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          37..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  36446 MW;  32AF7F82247164DB CRC64;
     MTARGGRAPL ARRAVVYGAV GLAAIAGVAM WSGAGRHGGT GASGEPPDAS AARGPAAAPP
     QAAVPASTSL PPSLAGSSAP RLPLDAGGHL AKARAVRDFF DYCLTAQSDL SAAGLDAFVM
     REIAAQLDGT VAQAEALDVW HRYRAYLDAL AKLRDAGAVD KSDLGALQLA LDQRASIAYR
     WLGDWSQPFF GAEQWRQRYD LARLKIAQDP ALTDAQKAER LAALEQQMPA DERAAQQRVD
     RQRAAIDQIA QLQKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQR RYADYAAQRA
     QIESAGLSPQ DRDAQIAALR QRVFTKPGEA VRAASLDRGA GSAR