ID   LIFO_VIBVY              Reviewed;         280 AA.
AC   Q7MK21;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=VV1989;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94753.1; -; Genomic_DNA.
DR   RefSeq; WP_011150534.1; NC_005139.1.
DR   AlphaFoldDB; Q7MK21; -.
DR   SMR; Q7MK21; -.
DR   STRING; 672.VV93_v1c17530; -.
DR   EnsemblBacteria; BAC94753; BAC94753; BAC94753.
DR   KEGG; vvy:VV1989; -.
DR   PATRIC; fig|196600.6.peg.2017; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_085683_0_0_6; -.
DR   OMA; QQYIDYK; -.
DR   OrthoDB; 1337848at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..280
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218489"
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   280 AA;  31895 MW;  DCAC3660FAD9DD34 CRC64;
     MKKTALTIIT IASGSLGAVY FLPSEPAVQK DIRATSQHDT SVDNTSPKAF LDYSLSTLGE
     KPWQTITQDV VSEERALGEL QLDEQLFALY LRYKQALADL DIEITGSDIT SLETLHQAIL
     DLQREYFSAQ QIDLIFGEEN QLRALALEKA RLSEQGYSAE EQKQLWRDHL ALQPEYVQES
     DANRRLMSEL AQGEDAQTTY LKRVELVGEA GAQRLEVLDQ NRAEFDRVFQ HYLVQRSAIL
     DDLGLSDEQK RQQIKMLRET SFDAKQWRRI EALERIADGG