LIFO_BURCM
ID LIFO_BURCM Reviewed; 344 AA.
AC Q0BAH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, 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=Bamb_3294;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000441; ABI88849.1; -; Genomic_DNA.
DR RefSeq; WP_011658335.1; NZ_CP009799.1.
DR AlphaFoldDB; Q0BAH4; -.
DR SMR; Q0BAH4; -.
DR STRING; 339670.Bamb_3294; -.
DR EnsemblBacteria; ABI88849; ABI88849; Bamb_3294.
DR GeneID; 44693945; -.
DR KEGG; bam:Bamb_3294; -.
DR PATRIC; fig|339670.21.peg.3500; -.
DR eggNOG; COG5380; Bacteria.
DR OMA; QQYIDYK; -.
DR Proteomes; UP000000662; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Lipase chaperone"
FT /id="PRO_1000046913"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
FT REGION 45..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 36602 MW; 0069CA2ECAE979C3 CRC64;
MTAREGRAPR VRRVAVYGAV GLAAIAGVAI WSGAASHRGA DTARLSADAA ARDGASAAPP
PPARPASAGM PSPLAGSSAP RLPLDAAGHL AKSRAVRDFF DYCLSARSDL SATALDALVV
REIAAQLDGT MAQPEALDVW HRYRAYLDAL AKLPDAGAVD KSDLGALQLA LDQRVSIAYR
TLGDWSQPFF GAEQWRQRYD LARLKIAQDR TLTEAQKAER LAALAQQMPG DERAARQKAD
RQQAAIDQIA QLQKSGATPD AMRAQLTQTL GPDAAARVAQ MQQDDASWQS RYADYAAQRA
QIEAAGLSPQ DRDAQIAALR QRMFTKPGEA VRAASLDRGA AAAR
