ID A0A031LN69_9CREN Unreviewed; 126 AA.
AC A0A031LN69;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CM19_09125 {ECO:0000313|EMBL:EZQ03870.1};
OS Candidatus Acidianus copahuensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=1160895 {ECO:0000313|EMBL:EZQ03870.1, ECO:0000313|Proteomes:UP000024332};
RN [1] {ECO:0000313|EMBL:EZQ03870.1, ECO:0000313|Proteomes:UP000024332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALE1 {ECO:0000313|EMBL:EZQ03870.1,
RC ECO:0000313|Proteomes:UP000024332};
RA Urbieta M.S., Rascovan N., Castro C., Revale S., Giaveno M.A.,
RA Vazquez M.P., Donati E.R.;
RT "Draft genome sequence of the novel thermoacidophilic archaea Acidianus
RT copahuensis ALE1 strain, isolated from Copahue volcanic area in Neuquen
RT Argentina.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EZQ03870.1}.
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DR EMBL; JFZT01000047; EZQ03870.1; -; Genomic_DNA.
DR RefSeq; WP_048100038.1; NZ_JFZT01000047.1.
DR AlphaFoldDB; A0A031LN69; -.
DR STRING; 1160895.CM19_09125; -.
DR OrthoDB; 204796at2157; -.
DR Proteomes; UP000024332; Unassembled WGS sequence.
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 CDD; cd00632; Prefoldin_beta; 1.
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 PANTHER; PTHR21431; PREFOLDIN SUBUNIT 6; 1.
DR PANTHER; PTHR21431:SF0; PREFOLDIN SUBUNIT 6; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00307};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00307};
KW Reference proteome {ECO:0000313|Proteomes:UP000024332}.
FT COILED 9..36
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 73..118
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 126 AA; 14774 MW; 007D6264E02270F8 CRC64;
MAERLPPDLQ TQLVKLQQLQ SQLDRLTYER SVIESELREV NKVLEELSMI STDSSVYKIV
GNVLLKKDKS SIEKELNDRK EILELRSRTY QKQESLLRKQ YEDLQKKINE LIQKYNLQGP
SSPPKA
//