ID A0A2H9LES8_9ARCH Unreviewed; 116 AA.
AC A0A2H9LES8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=COT14_01215 {ECO:0000313|EMBL:PIU22425.1};
OS Candidatus Diapherotrites archaeon CG08_land_8_20_14_0_20_30_16.
OC Archaea; Candidatus Diapherotrites.
OX NCBI_TaxID=1974403 {ECO:0000313|EMBL:PIU22425.1, ECO:0000313|Proteomes:UP000230520};
RN [1] {ECO:0000313|EMBL:PIU22425.1, ECO:0000313|Proteomes:UP000230520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG08_land_8_20_14_0_20_30_16 {ECO:0000313|EMBL:PIU22425.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) 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:PIU22425.1}.
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DR EMBL; PEXK01000021; PIU22425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9LES8; -.
DR Proteomes; UP000230520; 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 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}.
FT COILED 26..116
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 116 AA; 13268 MW; 818317D19FE37A5A CRC64;
MANISNEDFV AFNQYNAQLS SLNTQKTQIK MLIDSTQNAI EELKESKEDS AYKNLGFVML
KVEKGKLIQD LESEIETLNI RIKTLEKTEE VLSKKVQELQ AKLNAEMAKK DAKKEE
//
