(data stored in ACNUC1104 zone)

SWISSPROT: LIFO_BURCC

ID   LIFO_BURCC              Reviewed;         344 AA.
AC   B1K3P2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 59.
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=Bcenmc03_3611;
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the folding of the extracellular
CC       lipase during its passage through the periplasm.
CC       {ECO:0000255|HAMAP-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.
CC       {ECO:0000255|HAMAP-Rule:MF_00790}.
DR   EMBL; CP000959; ACA92763.1; -; Genomic_DNA.
DR   RefSeq; WP_011548118.1; NC_010515.1.
DR   SMR; B1K3P2; -.
DR   EnsemblBacteria; ACA92763; ACA92763; Bcenmc03_3611.
DR   KEGG; bcm:Bcenmc03_3611; -.
DR   HOGENOM; HOG000236502; -.
DR   OMA; QQYIDYK; -.
DR   BioCyc; BCEN406425:G1GBC-3834-MONOMER; -.
DR   Proteomes; UP000002169; 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;
DR   PRODOM; B1K3P2.
DR   SWISS-2DPAGE; B1K3P2.
KW   Cell inner membrane; Cell membrane; Chaperone; Complete proteome;
KW   Lipid degradation; Lipid metabolism; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    344       Lipase chaperone.
FT                                /FTId=PRO_1000190850.
FT   TRANSMEM     14     34       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00790}.
SQ   SEQUENCE   344 AA;  36239 MW;  BC45882BFA1010E4 CRC64;
     MAAREGRAPL ARRAAIYGVV GLAAIAGVAM WSGAGPHRGT GAAGDAPDAA AVGGVAAAAP
     QAAVPASAGL PPSLAGSSAP RLPLDAGGHL AKSRAVRDFF DYCLTARSDL SAAALDALVV
     REIAAQLDGT VAQVEALDVW HRYRAYLDAL ATLRDAGAVD KSDLGALQLA LDQRASIAYR
     TLGDWSQPFF GAEQWRQRYD LARLKITQDR SLTDAQKAER LAALQQQMPA DERAAQQRVD
     RQRAAIDQIA QLQKSGATPD AMRAQLTQTL GPEAAARVAQ MQQDDASWQS RYADYAAQRA
     QIESAGLSPQ DRDAQIAALR QRVFTKPGEA VRAASLDRGA GSAH
//

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