ID   PFDB_METBF              Reviewed;         117 AA.
AC   Q46FZ5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Mbar_A0213;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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}.
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DR   EMBL; CP000099; AAZ69197.1; -; Genomic_DNA.
DR   RefSeq; WP_011305252.1; NC_007355.1.
DR   AlphaFoldDB; Q46FZ5; -.
DR   SMR; Q46FZ5; -.
DR   STRING; 269797.Mbar_A0213; -.
DR   PRIDE; Q46FZ5; -.
DR   EnsemblBacteria; AAZ69197; AAZ69197; Mbar_A0213.
DR   GeneID; 3626304; -.
DR   KEGG; mba:Mbar_A0213; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_2_1_2; -.
DR   OMA; PPQVQAM; -.
DR   OrthoDB; 116327at2157; -.
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..117
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000232443"
SQ   SEQUENCE   117 AA;  13417 MW;  D0475A1209A285F2 CRC64;
     MTAELPPQIQ NQIAQLQQIQ QQIQALAMQK SQVEAMQKES KMALDELGRL ADDAVVYRNV
     GELVIKTSKE ESITKLKDRE ETLSLRLQSI SRQEERLTSR FKQLQEQIQQ ALGPRAQ