ID   A0A1I2MET5_9EURY        Unreviewed;       129 AA.
AC   A0A1I2MET5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=SAMN04488063_0715 {ECO:0000313|EMBL:SFF90005.1};
OS   Halopelagius inordinatus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=553467 {ECO:0000313|EMBL:SFF90005.1, ECO:0000313|Proteomes:UP000198876};
RN   [1] {ECO:0000313|Proteomes:UP000198876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7739 {ECO:0000313|Proteomes:UP000198876};
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; FOOQ01000001; SFF90005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2MET5; -.
DR   STRING; 553467.SAMN04488063_0715; -.
DR   OrthoDB; 204796at2157; -.
DR   Proteomes; UP000198876; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00307};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198876}.
FT   REGION          19..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14232 MW;  BCCA4C5D5A0D70C5 CRC64;
     MQGNLPPEAQ EKLEELQDLQ ETAQSVAAQK QQAESTLTES KTALETLEDV DEDTAMYREI
     GELLVETEYD EAYDDLEEKV DTLEVRVEQL QKQEERVQEQ FEDLQSELQQ MLQGGAGGGP
     MGPGGAGGA
//