ID   LIFO_VIBCM              Reviewed;         284 AA.
AC   C3LUP2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
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}; OrderedLocusNames=VCM66_A0218;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001234; ACP07197.1; -; Genomic_DNA.
DR   RefSeq; WP_000717572.1; NC_012580.1.
DR   AlphaFoldDB; C3LUP2; -.
DR   SMR; C3LUP2; -.
DR   EnsemblBacteria; ACP07197; ACP07197; VCM66_A0218.
DR   GeneID; 57741669; -.
DR   KEGG; vcm:VCM66_A0218; -.
DR   HOGENOM; CLU_085683_0_0_6; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000001217; Chromosome II.
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..284
FT                   /note="Lipase chaperone"
FT                   /id="PRO_1000148492"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ   SEQUENCE   284 AA;  32561 MW;  B0064285C85C0BC7 CRC64;
     MKKIAWSLGI LVTIGALCAI VWPSWYPSRP LVTTPSQADI QADQSSPRDL LEYFLSGLGE
     TSLPVIQQQV QRYEQENQGL LIDSSLFAQY VQYKAALSEL TLPQASGGLS TQEWWQLHQS
     LLDLQARYFS AEQQALFAEE NRLRELAIEK RRIYEQYGQS EEAQRAWQAL LLDQPDFIQR
     SEATAQLLPQ LTQAGQGDTQ QRYLARVALV GEQGAQRLAE LDDSRATFEQ QFQDYYQARA
     AILVRNELSA SEQQTQIQQL REQHFAPEQW RRIDALERLK DNGE