ID   LIFO_PSES5              Reviewed;         344 AA.
AC   P25276;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 75.
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;
DE   AltName: Full=Transcriptional activator act;
GN   Name=lifO; Synonyms=act, lipB;
OS   Pseudomonas sp. (strain KWI-56).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1368739; DOI=10.1271/bbb1961.55.2349;
RA   Iizumi T., Nakamura K., Shimada Y., Sugihara A., Tominaga Y., Fukase T.;
RT   "Cloning, nucleotide sequencing, and expression in Escherichia coli of a
RT   lipase and its activator genes from Pseudomonas sp. KWI-56.";
RL   Agric. Biol. Chem. 55:2349-2357(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; D10069; BAA00961.1; -; Genomic_DNA.
DR   EMBL; S77842; AAC60401.1; -; Genomic_DNA.
DR   AlphaFoldDB; P25276; -.
DR   SMR; P25276; -.
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_0000218485"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          39..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  36545 MW;  ABD9F8F68A44108B CRC64;
     MTSREGRAPL ARRAVVYGVV GLAAIAGVAM WSGAGWHRAT GASGESPEAS VAGGSVTAPP
     QAAVPASTGL PPSLAGSSAP RLPLDAGGHL AKSRAVRDFF DYCLTAQSDL SAAGLDAFVM
     REIAAQLDGT VAQAEALDVW HRYRAYLDAL AKLRDAGAAD KSDLGALQLA LDQRASIAYR
     TLGDWSQPFF GAEQWRQRYD LARLKIAQDP TLTDAQKAER LAALEQQMPA DERAAQQHID
     QQRAAIDQIA QLQKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQS RYADYAAQRT
     QIESAGLSPQ DRDAQIAALR QRVFTRPGEA VRAASLDRGA GSAR