ID   PFDB_PYRAB              Reviewed;         117 AA.
AC   Q9UYJ4; G8ZIT4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Prefoldin subunit beta;
DE   AltName: Full=GimC subunit beta;
GN   Name=pfdB; OrderedLocusNames=PYRAB15130; ORFNames=PAB1364;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AJ248287; CAB50418.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70967.1; -; Genomic_DNA.
DR   PIR; E75065; E75065.
DR   RefSeq; WP_010868631.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYJ4; -.
DR   SMR; Q9UYJ4; -.
DR   STRING; 272844.PAB1364; -.
DR   EnsemblBacteria; CAB50418; CAB50418; PAB1364.
DR   GeneID; 1495796; -.
DR   KEGG; pab:PAB1364; -.
DR   PATRIC; fig|272844.11.peg.1612; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_1_1_2; -.
DR   OMA; PPQVQAM; -.
DR   OrthoDB; 116327at2157; -.
DR   PhylomeDB; Q9UYJ4; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..117
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000124864"
SQ   SEQUENCE   117 AA;  13272 MW;  EF2BBB3369E856E3 CRC64;
     MQNIPPQVQA MLGQLESYQQ QLQLVIQQKQ KVQADLNEAK KALEEIEALP DDAQVYKTVG
     TLIVKTTKEK ALQELKEKVE TLEVRLNALN RQEQKINEKV KELTQKIQAA LRPPTAG