PFDB_PYRHO
ID PFDB_PYRHO Reviewed; 117 AA.
AC O58268;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Prefoldin subunit beta;
DE AltName: Full=GimC subunit beta;
GN Name=pfdB; OrderedLocusNames=PH0532;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 -!- INTERACTION:
CC O58268; O58263: pfdA; NbExp=2; IntAct=EBI-9014082, EBI-9014072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
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; BA000001; BAA29621.1; -; Genomic_DNA.
DR PIR; H71166; H71166.
DR RefSeq; WP_010884634.1; NC_000961.1.
DR PDB; 2ZDI; X-ray; 3.00 A; A/B=1-117.
DR PDBsum; 2ZDI; -.
DR AlphaFoldDB; O58268; -.
DR SMR; O58268; -.
DR DIP; DIP-29171N; -.
DR IntAct; O58268; 1.
DR STRING; 70601.3256938; -.
DR EnsemblBacteria; BAA29621; BAA29621; BAA29621.
DR GeneID; 1444421; -.
DR KEGG; pho:PH0532; -.
DR eggNOG; arCOG01342; Archaea.
DR OMA; PPQVQAM; -.
DR OrthoDB; 116327at2157; -.
DR EvolutionaryTrace; O58268; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm.
FT CHAIN 1..117
FT /note="Prefoldin subunit beta"
FT /id="PRO_0000124867"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2ZDI"
FT HELIX 15..47
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2ZDI"
FT HELIX 68..109
FT /evidence="ECO:0007829|PDB:2ZDI"
SQ SEQUENCE 117 AA; 13316 MW; FBF39C9878BDB427 CRC64;
MQNIPPQVQA MLGQLDTYQQ QLQLVIQQKQ KVQADLNEAK KALEEIETLP DDAQIYKTVG
TLIVKTTKEK AVQELKEKIE TLEVRLNALN RQEQKINEKV KELTQKIQAA LRPPTAG
