ID   LIFO_VIBCH              Reviewed;         284 AA.
AC   O07350;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=VC_A0222;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor O17 / Serotype O1;
RA   Manning P.A.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; Y00557; CAA68635.1; -; Genomic_DNA.
DR   EMBL; AE003853; AAF96134.1; -; Genomic_DNA.
DR   PIR; D82486; D82486.
DR   RefSeq; NP_232621.1; NC_002506.1.
DR   RefSeq; WP_000717572.1; NZ_LT906615.1.
DR   AlphaFoldDB; O07350; -.
DR   SMR; O07350; -.
DR   STRING; 243277.VC_A0222; -.
DR   DNASU; 2612551; -.
DR   EnsemblBacteria; AAF96134; AAF96134; VC_A0222.
DR   GeneID; 57741669; -.
DR   KEGG; vch:VC_A0222; -.
DR   PATRIC; fig|243277.26.peg.2855; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_085683_0_0_6; -.
DR   OMA; QQYIDYK; -.
DR   BioCyc; VCHO:VCA0222-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
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..284
FT                   /note="Lipase chaperone"
FT                   /id="PRO_0000218487"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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