ID   PFDB_METMP              Reviewed;         113 AA.
AC   Q6M0M5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=MMP0245;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(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}.
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DR   EMBL; BX950229; CAF29801.1; -; Genomic_DNA.
DR   RefSeq; WP_011170189.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0M5; -.
DR   SMR; Q6M0M5; -.
DR   STRING; 267377.MMP0245; -.
DR   EnsemblBacteria; CAF29801; CAF29801; MMP0245.
DR   GeneID; 41278667; -.
DR   KEGG; mmp:MMP0245; -.
DR   PATRIC; fig|267377.15.peg.248; -.
DR   eggNOG; arCOG01342; Archaea.
DR   HOGENOM; CLU_131909_0_1_2; -.
DR   OMA; PPQVQAM; -.
DR   OrthoDB; 123614at2157; -.
DR   BioCyc; MMAR267377:MMP_RS01335-MON; -.
DR   Proteomes; UP000000590; Chromosome.
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..113
FT                   /note="Prefoldin subunit beta"
FT                   /id="PRO_0000232442"
SQ   SEQUENCE   113 AA;  13478 MW;  69311CE205646398 CRC64;
     MELPANVQNQ LMQFQQLQQQ LQMIMYQKQQ FETQLKEMEK AIEEMEKSDS EEVFKMAGGI
     LVKRNKAEVK EELSEKIETL QLRVTTFEKQ EEKMQKRYTE LQESLQKVMG QGQ