ID A0A0F7DBI8_9EURY Unreviewed; 115 AA.
AC A0A0F7DBI8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Prefoldin subunit beta {ECO:0000256|ARBA:ARBA00016304, ECO:0000256|HAMAP-Rule:MF_00307};
DE AltName: Full=GimC subunit beta {ECO:0000256|ARBA:ARBA00033461, ECO:0000256|HAMAP-Rule:MF_00307};
GN Name=pfdB {ECO:0000256|HAMAP-Rule:MF_00307};
GN ORFNames=GAH_01546 {ECO:0000313|EMBL:AKG91166.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91166.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG91166.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG91166.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00025077,
CC ECO:0000256|HAMAP-Rule:MF_00307}.
CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC {ECO:0000256|ARBA:ARBA00011716, ECO:0000256|HAMAP-Rule:MF_00307}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00307}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|HAMAP-Rule:MF_00307}.
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DR EMBL; CP011267; AKG91166.1; -; Genomic_DNA.
DR RefSeq; WP_048095899.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7DBI8; -.
DR STRING; 113653.GAH_01546; -.
DR GeneID; 24804116; -.
DR KEGG; gah:GAH_01546; -.
DR HOGENOM; CLU_131909_1_1_2; -.
DR InParanoid; A0A0F7DBI8; -.
DR Proteomes; UP000034723; 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 NCBIfam; TIGR02338; gimC_beta; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00307};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00307};
KW Reference proteome {ECO:0000313|Proteomes:UP000034723}.
FT COILED 8..112
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 115 AA; 13118 MW; 87C51635C2CC95DE CRC64;
MGELPPQVQN LAAQLQQVQQ QLQLILTQKA QLESLIKEAK DALEELEKSD SDHAFKAVGN
VLVKLKKDEV EKDLKEKIET YEVRKNMLER QENKLRERLA DLQAKLKSAI NVQAG
//
