ID   TCPB_CAEEL              Reviewed;         529 AA.
AC   P47207; Q22628;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=T-complex protein 1 subunit beta;
DE            Short=TCP-1-beta;
DE   AltName: Full=CCT-beta;
GN   Name=cct-2; Synonyms=cctb; ORFNames=T21B10.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7576182; DOI=10.1089/dna.1995.14.951;
RA   Leroux M.R., Candido E.P.M.;
RT   "Characterization of four new tcp-1-related cct genes from the nematode
RT   Caenorhabditis elegans.";
RL   DNA Cell Biol. 14:951-960(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- INTERACTION:
CC       P47207; G5EEN7: CELE_Y39A1A.3; NbExp=4; IntAct=EBI-896048, EBI-2412943;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U25632; AAA93233.1; -; mRNA.
DR   EMBL; Z68318; CAA92697.1; -; Genomic_DNA.
DR   EMBL; AL031268; CAA92697.1; JOINED; Genomic_DNA.
DR   PIR; T18589; T18589.
DR   RefSeq; NP_741031.1; NM_171985.5.
DR   AlphaFoldDB; P47207; -.
DR   SMR; P47207; -.
DR   BioGRID; 39748; 15.
DR   IntAct; P47207; 3.
DR   STRING; 6239.T21B10.7; -.
DR   World-2DPAGE; 0011:P47207; -.
DR   EPD; P47207; -.
DR   PaxDb; P47207; -.
DR   PeptideAtlas; P47207; -.
DR   EnsemblMetazoa; T21B10.7.1; T21B10.7.1; WBGene00000378.
DR   GeneID; 174421; -.
DR   KEGG; cel:CELE_T21B10.7; -.
DR   UCSC; T21B10.7.1; c. elegans.
DR   CTD; 174421; -.
DR   WormBase; T21B10.7; CE16437; WBGene00000378; cct-2.
DR   eggNOG; KOG0363; Eukaryota.
DR   GeneTree; ENSGT00550000074930; -.
DR   HOGENOM; CLU_008891_6_2_1; -.
DR   InParanoid; P47207; -.
DR   OMA; YCTGGEI; -.
DR   OrthoDB; 335406at2759; -.
DR   PhylomeDB; P47207; -.
DR   BRENDA; 3.6.4.B10; 1045.
DR   Reactome; R-CEL-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P47207; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000378; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03336; TCP1_beta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012716; Chap_CCT_beta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   PANTHER; PTHR11353:SF23; PTHR11353:SF23; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02341; chap_CCT_beta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..529
FT                   /note="T-complex protein 1 subunit beta"
FT                   /id="PRO_0000128318"
FT   CONFLICT        427
FT                   /note="A -> S (in Ref. 1; AAA93233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   529 AA;  56975 MW;  07806C9AF26D79B2 CRC64;
     MLPVQILKDN AQEERGESAR LSSFVGAIAI GDLVKSTLGP KGMDKILISG NPESAGGIKV
     TNDGATILKS IGVDNPAAKV LVDMSMTQDH EVGDGTTSVT VLAAELLKEA EKLVNQRIHP
     QTIISGYRRA LGIAQESLKK SSIESGDNIR DDLLKIARTT LGSKILSQHK EHFAQLAVDA
     VLRLKGSGNL DAIQIIKKLG GSMNESYLDE GFLLEKLPGM FQPRRVEKAK ILIANTPMDT
     DKVKVFGSRV RVDGVAKVAE LEAAEKLKMK EKVDKILAHN CNVFINRQLI YNYPEQLFAD
     AKVMAIEHAD FEGIERLALV LGGEIVSTFD SPQTAQFGSC DLIEEIMIGE DRLLRFSGVK
     LGEACSVVLR GATQQILDES ERSLHDALCV LVTHVKESKT VAGAGASEIL MSSAIAVEAQ
     KVAGKEALAV EAFGRALAQL PTIICDNAGL DSAELVTRLR AEHANGRHNM GIDIEKGEVA
     DVTKLGVIES YNVKLCMVSS AAEATEQILR VDDIIKAAPR ARAQDNRPC