ID   LIFO_XYLF2              Reviewed;         353 AA.
AC   B2I8J9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Lipase chaperone {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase activator protein {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase foldase {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase helper protein {ECO:0000255|HAMAP-Rule:MF_00790};
DE   AltName: Full=Lipase modulator {ECO:0000255|HAMAP-Rule:MF_00790};
GN   Name=lifO {ECO:0000255|HAMAP-Rule:MF_00790};
GN   OrderedLocusNames=XfasM23_0463;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
CC   -!- FUNCTION: May be involved in the folding of the extracellular lipase
CC       during its passage through the periplasm. {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00790}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
CC   -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00790}.
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DR   EMBL; CP001011; ACB91910.1; -; Genomic_DNA.
DR   RefSeq; WP_011097653.1; NC_010577.1.
DR   AlphaFoldDB; B2I8J9; -.
DR   SMR; B2I8J9; -.
DR   PRIDE; B2I8J9; -.
DR   EnsemblBacteria; ACB91910; ACB91910; XfasM23_0463.
DR   GeneID; 58016014; -.
DR   KEGG; xfn:XfasM23_0463; -.
DR   HOGENOM; CLU_064928_1_0_6; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000001698; 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_1000190852"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
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