ID A0A1H3CYY4_9EURY Unreviewed; 129 AA.
AC A0A1H3CYY4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04487946_101246 {ECO:0000313|EMBL:SDX58754.1};
OS Halobellus clavatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=660517 {ECO:0000313|EMBL:SDX58754.1, ECO:0000313|Proteomes:UP000199170};
RN [1] {ECO:0000313|Proteomes:UP000199170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10118 {ECO:0000313|Proteomes:UP000199170};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNPB01000001; SDX58754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3CYY4; -.
DR STRING; 660517.SAMN04487946_101246; -.
DR OrthoDB; 204796at2157; -.
DR Proteomes; UP000199170; 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 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; PTHR20903:SF0; PREFOLDIN SUBUNIT 1; 1.
DR PANTHER; PTHR20903; PREFOLDIN SUBUNIT 1-RELATED; 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|HAMAP-Rule:MF_00307};
KW Reference proteome {ECO:0000313|Proteomes:UP000199170}.
FT COILED 9..114
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 129 AA; 14177 MW; 0CF59DEF5896B07F CRC64;
MQGNLPPEAQ EKLEELQDLQ DTAQKVAAQK EQAESTLTES KTALEALEEI DEGTTMYREV
GELLVETEYD EAHEELDDKV DSLEIRVEQL TKQEERVEEQ FESLQQELQQ MLQGGAGGGP
MGPGGAGGA
//
