ID   LIFO_BURL3              Reviewed;         344 AA.
AC   Q393T3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Bcep18194_B2172;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000152; ABB12283.1; -; Genomic_DNA.
DR   RefSeq; WP_011355766.1; NC_007511.1.
DR   AlphaFoldDB; Q393T3; -.
DR   SMR; Q393T3; -.
DR   PRIDE; Q393T3; -.
DR   EnsemblBacteria; ABB12283; ABB12283; Bcep18194_B2172.
DR   GeneID; 45098499; -.
DR   KEGG; bur:Bcep18194_B2172; -.
DR   PATRIC; fig|482957.22.peg.5929; -.
DR   HOGENOM; CLU_064928_1_0_4; -.
DR   OMA; QQYIDYK; -.
DR   OrthoDB; 1337848at2; -.
DR   Proteomes; UP000002705; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..344
FT                   /note="Lipase chaperone"
FT                   /id="PRO_1000046914"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ   SEQUENCE   344 AA;  36556 MW;  6C286993151BC3EB CRC64;
     MTARGGRAPL ARRAMVYGVV GLAAIAGVAM WSGASWHRGT GAASDSPDAP VAGGLAAAPP
     QAAVPASAGL PPSLAGSSAP RLPLDAGGHL AKSRAVRDFF DYCLTAQSDL SAAALDAFVV
     REIAAQLDGT VAQVEALDVW HRYRAYLDAL AKLRDAGAVD KSDLGALQLA LDQRASIAYR
     TLGDWSQPFF GAEQWRQRYD LARLKITRDP TLTDAQKAER LAALEQQMPA DERAAQKRID
     KQRAAIDQIA QLQKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQS RYTDYAAQRA
     QIESAGLSPQ DRDAQITALR QRVFTKPGEA VRAASLDRGA GSAR