PFDB_METM5
ID PFDB_METM5 Reviewed; 113 AA.
AC A4FZU2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Prefoldin subunit beta {ECO:0000255|HAMAP-Rule:MF_00307};
DE AltName: Full=GimC subunit beta {ECO:0000255|HAMAP-Rule:MF_00307};
GN Name=pfdB {ECO:0000255|HAMAP-Rule:MF_00307}; OrderedLocusNames=MmarC5_1428;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone capable of stabilizing a range of
CC proteins. Seems to fulfill an ATP-independent, HSP70-like function in
CC archaeal de novo protein folding. {ECO:0000255|HAMAP-Rule:MF_00307}.
CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00307}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00307}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000255|HAMAP-Rule:MF_00307}.
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; CP000609; ABO35726.1; -; Genomic_DNA.
DR RefSeq; WP_011869176.1; NC_009135.1.
DR AlphaFoldDB; A4FZU2; -.
DR SMR; A4FZU2; -.
DR STRING; 402880.MmarC5_1428; -.
DR EnsemblBacteria; ABO35726; ABO35726; MmarC5_1428.
DR GeneID; 4928687; -.
DR KEGG; mmq:MmarC5_1428; -.
DR eggNOG; arCOG01342; Archaea.
DR HOGENOM; CLU_131909_0_1_2; -.
DR OMA; PPQVQAM; -.
DR OrthoDB; 123614at2157; -.
DR Proteomes; UP000000253; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.370; -; 1.
DR HAMAP; MF_00307; PfdB; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR012713; PfdB.
DR InterPro; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 1.
DR TIGRFAMs; TIGR02338; gimC_beta; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm.
FT CHAIN 1..113
FT /note="Prefoldin subunit beta"
FT /id="PRO_1000022793"
SQ SEQUENCE 113 AA; 13391 MW; 84A99D47CF61F8C2 CRC64;
MELPANVQNQ LMQFQQLQQQ LQMIMYQKQQ FETQLKEMEK AIEEMEKSGS DEVFKMAGGI
LIKRNKAEVK EELSEKVETL QVRVTTFEKQ EEKMQKRYTE LQESLQKVMG QGQ