ID   PFDB_METMJ              Reviewed;         121 AA.
AC   A3CW49;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Memar_1672;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57599.1; -; Genomic_DNA.
DR   RefSeq; WP_011844510.1; NC_009051.1.
DR   AlphaFoldDB; A3CW49; -.
DR   SMR; A3CW49; -.
DR   STRING; 368407.Memar_1672; -.
DR   EnsemblBacteria; ABN57599; ABN57599; Memar_1672.
DR   GeneID; 4846674; -.
DR   KEGG; mem:Memar_1672; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_0_0_2; -.
DR   OMA; PPQVQAM; -.
DR   OrthoDB; 111665at2157; -.
DR   Proteomes; UP000002146; 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..121
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000300774"
SQ   SEQUENCE   121 AA;  13632 MW;  3D2D3BB8203F939B CRC64;
     MENIPPKVQN QLAMLQQMQQ QLQTVVSQKG QYELTIREAR RAVEDLADVP EDAAVFMNVG
     SVMMQKSKEQ VLASLNERIE TLELRVKSLE KQEKALQGRF EQLSSQIRGA LEGKQQPPGP
     A