LIFO_PSEAE
ID LIFO_PSEAE Reviewed; 340 AA.
AC Q01725; P95420; Q04591;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 4.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Lipase chaperone;
DE AltName: Full=Lipase foldase;
DE AltName: Full=Lipase helper protein;
DE AltName: Full=Lipase modulator;
GN Name=lifO; Synonyms=lipB, lipH; OrderedLocusNames=PA2863;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TE3285;
RX PubMed=1632642; DOI=10.1016/0003-9861(92)90604-u;
RA Chihara-Siomi M., Yoshikawa K., Oshima-Hirayama N., Yamamoto K., Sogabe Y.,
RA Nakatani T., Nishioka T., Oda J.;
RT "Purification, molecular cloning, and expression of lipase from Pseudomonas
RT aeruginosa.";
RL Arch. Biochem. Biophys. 296:505-513(1992).
RN [2]
RP SEQUENCE REVISION.
RA Shibata H.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31156 / FERM-P 2611;
RX PubMed=8982856; DOI=10.1093/oxfordjournals.jbchem.a021506;
RA Shinkai A., Hirano A., Aisaka K.;
RT "Substitutions of Ser for Asn-163, and Pro for Leu-264 are important for
RT stabilization of lipase from Pseudomonas aeruginosa.";
RL J. Biochem. 120:915-921(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1512563; DOI=10.1099/00221287-138-7-1325;
RA Wohlfarth S., Hoesche C., Strunk C., Winkler U.K.;
RT "Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa
RT PAO1.";
RL J. Gen. Microbiol. 138:1325-1335(1992).
RN [5]
RP SEQUENCE REVISION.
RA Wohlfarth S.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG06251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA44998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB008452; BAA23129.1; -; Genomic_DNA.
DR EMBL; D50588; BAA09136.1; -; Genomic_DNA.
DR EMBL; X63391; CAA44998.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG06251.1; ALT_INIT; Genomic_DNA.
DR PIR; C83289; C83289.
DR PIR; S24161; S24161.
DR PIR; S25769; S25769.
DR RefSeq; NP_251553.1; NC_002516.2.
DR PDB; 5OVM; NMR; -; A=66-146.
DR PDB; 6GSF; NMR; -; A=66-146.
DR PDBsum; 5OVM; -.
DR PDBsum; 6GSF; -.
DR AlphaFoldDB; Q01725; -.
DR SMR; Q01725; -.
DR STRING; 287.DR97_5078; -.
DR PaxDb; Q01725; -.
DR PRIDE; Q01725; -.
DR DNASU; 882663; -.
DR EnsemblBacteria; AAG06251; AAG06251; PA2863.
DR GeneID; 882663; -.
DR KEGG; pae:PA2863; -.
DR PATRIC; fig|208964.12.peg.3003; -.
DR PseudoCAP; PA2863; -.
DR HOGENOM; CLU_064928_0_0_6; -.
DR OMA; QQYIDYK; -.
DR Proteomes; UP000002438; 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:0044248; P:cellular catabolic process; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone;
KW Lipid degradation; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Lipase chaperone"
FT /id="PRO_0000218483"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 210
FT /note="A -> T (in strain: TE3285 and ATCC 31156)"
FT VARIANT 301
FT /note="T -> A (in strain: TE3285 and ATCC 31156)"
FT CONFLICT 41..42
FT /note="DR -> VH (in Ref. 6)"
FT /evidence="ECO:0000305"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5OVM"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6GSF"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6GSF"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:5OVM"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6GSF"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:5OVM"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:5OVM"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:5OVM"
SQ SEQUENCE 340 AA; 37687 MW; 55217FCDF8FFC251 CRC64;
MKKILLLIPL AFAASLAWFV WLEPSPAPET APPASPQAGA DRAPPAASAG EAVPAPQVMP
AKVAPLPTSF RGTSVDGSFS VDASGNLLIT RDIRNLFDYF LSAVGEEPLQ QSLDRLRAYI
AAELQEPARG QALALMQQYI DYKKELVLLE RDLPRLADLD ALRQREAAVK ALRARIFSNE
AHVAFFADEE TYNQFTLERL AIRQDGKLSA EEKAAAIDRL RASLPEDQQE SVLPQLQSEL
QQQTAALQAA GAGPEAIRQM RQQLVGAEAT TRLEQLDRQR SAWKGRLDDY FAEKSRIEGN
TGLSEADRRA AVERLAEERF SEQERLRLGA LEQMRQAEQR
