ID   LIFO_PSEU5              Reviewed;         335 AA.
AC   A4VL35;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=PST_2015;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000304; ABP79686.1; -; Genomic_DNA.
DR   RefSeq; WP_011913156.1; NC_009434.1.
DR   AlphaFoldDB; A4VL35; -.
DR   SMR; A4VL35; -.
DR   STRING; 379731.PST_2015; -.
DR   EnsemblBacteria; ABP79686; ABP79686; PST_2015.
DR   KEGG; psa:PST_2015; -.
DR   eggNOG; COG5380; Bacteria.
DR   HOGENOM; CLU_064928_0_0_6; -.
DR   OMA; QQYIDYK; -.
DR   Proteomes; UP000000233; 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..335
FT                   /note="Lipase chaperone"
FT                   /id="PRO_1000046916"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ   SEQUENCE   335 AA;  37146 MW;  0574E7C6F887583A CRC64;
     MSGSILLLPL AIALGLGFFI ARPESTVTPV AEAPTSSPAA NLTAARPAQR TATGAAPQVT
     AKLPASFKGT EVDGQFQLDA AGNLIIGPEL RQLFDYFLSA IGEEPLKQSI ERLRRHIAAQ
     LPEPAQAQAL AVLNQYLNYK RQLVDFEAQH PRVADLASMR DRLSAVRALR AHALDPATHQ
     AFFGLEEAYD HFSLERLAIR FDPALDSDAK GRAIDQLRAG LPAELQDLLM PQLQTELREQ
     TTALLANGAG PQQLRQLRQQ LVGSEAADRL EALDLQRRQW QQRVASYQQE RTRIETARGL
     DEVERRAAVE RLEAQRFSDS ERLRLLAVVQ EDRTR