ID   LIFO_ACIVR              Reviewed;         346 AA.
AC   Q9X2S4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, 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;
GN   Name=lifO; Synonyms=lipB;
OS   Acinetobacter venetianus (strain ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG
OS   45561 / CIP 110063 / KCTC 2702 / LMG 19082 / RAG-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1191460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG 45561 / CIP 110063 / KCTC
RC   2702 / LMG 19082 / RAG-1;
RX   PubMed=10216267; DOI=10.1016/s0378-1119(99)00026-8;
RA   Sullivan E.R., Leahy J.G., Colwell R.R.;
RT   "Cloning and sequence analysis of the lipase and lipase chaperone-encoding
RT   genes from Acinetobacter calcoaceticus RAG-1, and redefinition of a
RT   proteobacterial lipase family and an analogous lipase chaperone family.";
RL   Gene 230:277-285(1999).
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; AF047691; AAD29442.1; -; Genomic_DNA.
DR   RefSeq; WP_004880062.1; NZ_KB849558.1.
DR   AlphaFoldDB; Q9X2S4; -.
DR   SMR; Q9X2S4; -.
DR   GeneID; 58195044; -.
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..346
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218478"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   346 AA;  38583 MW;  98218A6C5363FBEB CRC64;
     MSGKFINHKT IVFGVITSVL LLLLLIYYVF KPEAQTQNQN INTQTIQPEN TVLESATANN
     KQGKLPTLAA SLQGTEIDCP IQVDANGKLI LTVGIRSCFD YFFSSLGEKT EAELVADIRQ
     YLLATLPESA SNYAIYLLDQ YVAYMHALQN LKPNAGFKSN NVDALQKVVD QMAKVQQQFF
     NAAEINALFG NERNLNQFNL EQMRIHANKN LTTQEKATEL AKLIDELPPA LADGVRVSMQ
     FAELQQLTKE IQAKGGSAQD LRSMRESLLG PEAADRLEKV DQEEAVWQTQ VNQYLSARDQ
     ILKSDANDAS KQQSIAELRN SSFGTKEDLL RAQSYEVMHD QKSKGS