ID   LIFO_CHRVO              Reviewed;         303 AA.
AC   Q7NUI5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=lipH; OrderedLocusNames=CV_2713;
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC   9757;
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA   Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA   Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA   Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA   Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA   Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA   Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA   de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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; AE016825; AAQ60383.1; -; Genomic_DNA.
DR   RefSeq; WP_011136260.1; NC_005085.1.
DR   AlphaFoldDB; Q7NUI5; -.
DR   SMR; Q7NUI5; -.
DR   STRING; 243365.CV_2713; -.
DR   PRIDE; Q7NUI5; -.
DR   EnsemblBacteria; AAQ60383; AAQ60383; CV_2713.
DR   KEGG; cvi:CV_2713; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_064928_0_0_4; -.
DR   OMA; QQYIDYK; -.
DR   OrthoDB; 1337848at2; -.
DR   Proteomes; UP000001424; Chromosome.
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..303
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218482"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  33275 MW;  BAFC18276DE34B8E CRC64;
     MRGLGLTLAA ACAAWLAWWA WPDGAHSEAA AARQAARGGF APSLIGTRPD GAAAEADGKL
     VVDQQLRQLF DYYLATLGER DLAVIRTELQ GQLKRSLKNG PLAQAMGLFD RYVGYKRSLA
     GKAAAAATDL SHRLELVQAA RRQYFSQAEL DGLFGDEDRY DNFTARRLAI EANPALSVDE
     KRRRVAQLEQ QLPPGLRAAR EEPVKHLALA DAEARLRQGG GGEQQLYQLR AGMVGQAAAD
     RLGELDREQA AWQNRVDDFK RERTAILADG GLSAQQRQQA LARLQAQRFS QQESLRLPAY
     LSN