LIFO_VIBC3
ID LIFO_VIBC3 Reviewed; 284 AA.
AC A5EYU0; C3M7V4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=VC0395_1005, VC395_A0259;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
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}; Periplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00790}.
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DR EMBL; CP000626; ABQ19343.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11100.1; -; Genomic_DNA.
DR RefSeq; WP_000717572.1; NZ_JAACZH010000027.1.
DR AlphaFoldDB; A5EYU0; -.
DR SMR; A5EYU0; -.
DR STRING; 345073.VC395_A0259; -.
DR EnsemblBacteria; ABQ19343; ABQ19343; VC0395_1005.
DR GeneID; 57741669; -.
DR KEGG; vco:VC0395_1005; -.
DR KEGG; vcr:VC395_A0259; -.
DR PATRIC; fig|345073.21.peg.3021; -.
DR eggNOG; COG5380; Bacteria.
DR HOGENOM; CLU_085683_0_0_6; -.
DR OMA; QQYIDYK; -.
DR Proteomes; UP000000249; Chromosome 1.
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_1000072840"
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
