ID   LIFO_BURCJ              Reviewed;         344 AA.
AC   B4EF95;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=BceJ2315_44050; ORFNames=BCAM0950;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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}.
CC   -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
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DR   EMBL; AM747721; CAR54807.1; -; Genomic_DNA.
DR   RefSeq; WP_006493459.1; NC_011001.1.
DR   AlphaFoldDB; B4EF95; -.
DR   SMR; B4EF95; -.
DR   STRING; 216591.BCAM0950; -.
DR   EnsemblBacteria; CAR54807; CAR54807; BCAM0950.
DR   KEGG; bcj:BCAM0950; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_064928_1_0_4; -.
DR   OMA; QQYIDYK; -.
DR   OrthoDB; 1337848at2; -.
DR   BioCyc; BCEN216591:G1G1V-4939-MON; -.
DR   Proteomes; UP000001035; 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_1000190851"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ   SEQUENCE   344 AA;  36356 MW;  79FDA4D6B7D37157 CRC64;
     MAAREGRAPL VRRAAIYGGV GLAAVAGVAM WSGAGSHRGT GAAGDAPEAA AVGGVAVAAS
     QAAVPASAGV PPSLAGSSAP RLPLDAGGHL AKSRTVRDFF DYCLTARSDL SAAALDAFVV
     REIAAQLDGT VAQAEALDVW HRYRAYLDAL ATLRDAGAVD KSDPGALQLA LDQRASIAYR
     TLGDWSQPFF GAEQWRQRYD LARLKITQDR SLTDAQKAER LAALEQQMPA DEREAQQRVD
     RQRAAIDQIA QLRKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQS RYADYAAQRT
     QIESAGLSPQ DRDAQIAALR QRVFTKPGEA VRAASLDRGA GSAH