ID   LIFO_VIBVU              Reviewed;         280 AA.
AC   Q8DA60;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
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; OrderedLocusNames=VV1_2350;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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: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; AE016795; AAO10724.1; -; Genomic_DNA.
DR   RefSeq; WP_011080218.1; NC_004459.3.
DR   AlphaFoldDB; Q8DA60; -.
DR   SMR; Q8DA60; -.
DR   EnsemblBacteria; AAO10724; AAO10724; VV1_2350.
DR   KEGG; vvu:VV1_2350; -.
DR   HOGENOM; CLU_085683_0_0_6; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..280
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218488"
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   280 AA;  31829 MW;  9068A0CC2D99A3B4 CRC64;
     MKKTALTIIT IALGSLGAVY FLPSEPAAQK DIRATSQHDT SVDNTSAKAF LDYSLSTLGE
     KPLQTITQDV VREERALGEL QLDEQLFALY LRYKQALADL DIEITGSDII SLETLHQAIL
     DLQREYFSAQ QIDLIFGEEN QLRALALEKA RLSEQGYSAE EQKQLWRDHL ALQPEYVQES
     DANRRLMSEL AQGEDAQTTY LKRVELVGEA GAQRLEVLDQ NRAEFDRVFQ HYLVQRSAIL
     DDLGLSDEQK HKQITMLRET SFDAKQWRRI EALERIADGG