LIFO_BURA4
ID LIFO_BURA4 Reviewed; 344 AA.
AC B1Z1J6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=BamMC406_3810;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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}.
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; CP001026; ACB66277.1; -; Genomic_DNA.
DR RefSeq; WP_012365663.1; NC_010552.1.
DR AlphaFoldDB; B1Z1J6; -.
DR SMR; B1Z1J6; -.
DR EnsemblBacteria; ACB66277; ACB66277; BamMC406_3810.
DR KEGG; bac:BamMC406_3810; -.
DR HOGENOM; CLU_064928_1_0_4; -.
DR OMA; QQYIDYK; -.
DR OrthoDB; 1337848at2; -.
DR Proteomes; UP000001680; 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_1000190849"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00790"
SQ SEQUENCE 344 AA; 36384 MW; 9FBB2F6CCF76531B CRC64;
MTAREGRAPL VRRVAVYGAV GLAAIAGVAI WSGAASHRGA DTARLSADAA ARDGASAASP
PPALPASAGL PAPLAGSSAP RLPLDAGGHL AKSRAVRDFF DYCLSARSDL SATALDALVV
RGIAAQLDGT IAQPEALDVW HRYRAYLDAL AKLPDAGAVD KSDLGALQLA LDQRVSIAYR
TLGDWSQPFF GAEQWRQRYD LARLKIAQDR TLTEAQKAER LAALAQQMPA DERAARQKAD
RQQAAIDQIA QLQKSGATPD AMRAQLTQTL GPDAAARVAQ MQQDDASWQS RYADYAAQRA
QIDAAGLSPQ DRDAQIASLR QRMFTKPGEA VRAASLDRGA AAAR