LIFO_ACIAD
ID LIFO_ACIAD Reviewed; 343 AA.
AC Q43961; Q6F7I4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=ACIAD3308;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7768830; DOI=10.1128/jb.177.11.3295-3307.1995;
RA Kok R.G., Thor J.J., Nugteren-Roodzant I.M., Vosman B., Hellingwerf K.J.;
RT "Characterization of lipase-deficient mutants of Acinetobacter
RT calcoaceticus BD413: identification of a periplasmic lipase chaperone
RT essential for the production of extracellular lipase.";
RL J. Bacteriol. 177:3295-3307(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: May be involved in the folding of the extracellular lipase
CC during its passage through the periplasm.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein; Periplasmic side.
CC -!- SIMILARITY: Belongs to the lipase chaperone family. {ECO:0000305}.
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DR EMBL; X80800; CAA56779.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG69981.1; -; Genomic_DNA.
DR PIR; A57253; A57253.
DR RefSeq; WP_004923856.1; NC_005966.1.
DR AlphaFoldDB; Q43961; -.
DR SMR; Q43961; -.
DR STRING; 62977.ACIAD3308; -.
DR EnsemblBacteria; CAG69981; CAG69981; ACIAD3308.
DR GeneID; 45235509; -.
DR KEGG; aci:ACIAD3308; -.
DR eggNOG; COG5380; Bacteria.
DR HOGENOM; CLU_064928_2_0_6; -.
DR OMA; QQYIDYK; -.
DR OrthoDB; 1337848at2; -.
DR BioCyc; ASP62977:ACIAD_RS14970-MON; -.
DR Proteomes; UP000000430; 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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..343
FT /note="Lipase chaperone"
FT /id="PRO_0000218477"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 322
FT /note="D -> V (in Ref. 1; CAA56779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 39016 MW; 0613A58CEE5EC719 CRC64;
MNGSKKIYLG IGLVALLMIF IYWLMPKDTA NASSQIESTN ASAIIATSPG QQNQLSENTT
PFGSVSQHDT QVNCQLQLNA ANHLIVNEQT RNCFEYFLTQ YGEKSLTQID QDIKNYFTQS
LPQPARDQAQ DLWQRYLKYR EELGNLKEPA IAKTDIAYYR AVFTSRQMLR QRFFSATEIA
GLFGSEDIYN QYTLERMAIL NNSKLSEIEK AKQLKALFDQ LPQDWKANLE QLSKLDDLKQ
LTTSIKKNGG SAQELHDMRT NLVGHDATAR LEQLDVERSN WKSNVTQYLD ERQTILNSNM
SDTAKQNAIS ALRSKNFTAP QDQIRVQAFE SAKDQGQSLP FSE
