ID   PFDB_HALMA              Reviewed;         129 AA.
AC   Q5V1L3;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Prefoldin subunit beta {ECO:0000255|HAMAP-Rule:MF_00307};
DE   AltName: Full=GimC subunit beta {ECO:0000255|HAMAP-Rule:MF_00307};
GN   Name=pfdB {ECO:0000255|HAMAP-Rule:MF_00307}; OrderedLocusNames=rrnAC1680;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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:0000255|HAMAP-Rule:MF_00307}.
CC   -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00307}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00307}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000255|HAMAP-Rule:MF_00307}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV46589.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY596297; AAV46589.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004591484.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V1L3; -.
DR   SMR; Q5V1L3; -.
DR   STRING; 272569.rrnAC1680; -.
DR   EnsemblBacteria; AAV46589; AAV46589; rrnAC1680.
DR   GeneID; 40152642; -.
DR   GeneID; 64821750; -.
DR   KEGG; hma:rrnAC1680; -.
DR   PATRIC; fig|272569.17.peg.2366; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_0_1_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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   TIGRFAMs; TIGR02338; gimC_beta; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..129
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000232441"
FT   REGION          19..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14161 MW;  6C48E2BFB2685B2D CRC64;
     MQGNLPPEAQ EKLEELQDLQ QTAQQVAAQK QQAETELQES QTALDELDDI DEDSTMYREV
     GELLVKTEFD EAQDDLEEKV NSLEVRVETL EKQEERVQEQ FEELQSELQQ MLGGAGGAGP
     AGGPGAGGA