ID   LIFO_XYLFT              Reviewed;         353 AA.
AC   Q87E55;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 91.
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; OrderedLocusNames=PD_0466;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(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; AE009442; AAO28345.1; -; Genomic_DNA.
DR   RefSeq; WP_011097653.1; NC_004556.1.
DR   AlphaFoldDB; Q87E55; -.
DR   SMR; Q87E55; -.
DR   EnsemblBacteria; AAO28345; AAO28345; PD_0466.
DR   GeneID; 58016014; -.
DR   KEGG; xft:PD_0466; -.
DR   HOGENOM; CLU_064928_1_0_6; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000002516; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218491"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  39998 MW;  15B13D272731C97D CRC64;
     MIKKYSFVNH RIVLYLILGC VVVCGVWYSF DVRQAIDVGA VDLSLPQMSN NLLKEVAVGE
     GKTTNRLSRL PVDSTVPTVL PQSLAGSIAP PLPLDAYGHL ARVSAVRDFF DYFLTAQNDL
     TPAALDEIVT HEIVKQLHGK SAQAEAQDVW TRYCAYFSQL VKLPDMGMVL GDKLDFVAVQ
     RALDQRASLA VRTLGDWSEP FFGAEQQRQR YDLERLKIAD DQALTDEQKK KRLVALEQKL
     PSKVQEERIK IQQQQDAVVK IIQLQKDEVT PDGIRLQVVG LLGPEVAYRV AEIRRQDEIW
     QEKYKHYAAQ RAQRAQIEAQ QLEPKEHDVQ VENLRQRIFT KPGEALRAAS LDQ