ID   PFDB_NATPD              Reviewed;         131 AA.
AC   Q3ITY6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=NP_0612A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48397.1; -; Genomic_DNA.
DR   RefSeq; WP_011322033.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITY6; -.
DR   SMR; Q3ITY6; -.
DR   STRING; 348780.NP_0612A; -.
DR   EnsemblBacteria; CAI48397; CAI48397; NP_0612A.
DR   GeneID; 3703018; -.
DR   KEGG; nph:NP_0612A; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_0_1_2; -.
DR   OMA; PPQVQAM; -.
DR   OrthoDB; 116327at2157; -.
DR   Proteomes; UP000002698; 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; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000232444"
FT   REGION          19..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  14455 MW;  58C11D09402CD7A6 CRC64;
     MQGNLPPEAQ EKIEELQDLQ ETAQQVAQQK QQAETQLRES ETALETLDDI EGDTQMYQEV
     GELLIETDYD EAYENLEEKV DSLEVRVETL TKQEERVQDQ FEGLQEELQE MLQGGAGGGP
     MGPGGPGAGG A