THSB_SULAC
ID THSB_SULAC Reviewed; 553 AA.
AC Q9V2T4; Q4JAX9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Thermosome subunit beta;
DE AltName: Full=Chaperonin subunit beta;
DE AltName: Full=Thermophilic factor 55 beta;
DE Short=TF55-beta;
DE AltName: Full=Thermosome subunit 2;
GN Name=thsB; OrderedLocusNames=Saci_0666;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-509.
RX PubMed=10508614; DOI=10.1016/s0960-9822(99)80457-6;
RA Archibald J.M., Logsdon J.M. Jr., Doolittle W.F.;
RT "Recurrent paralogy in the evolution of archaeal chaperonins.";
RL Curr. Biol. 9:1053-1056(1999).
CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC and has a weak ATPase activity. {ECO:0000250}.
CC -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC rings. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; CP000077; AAY80050.1; -; Genomic_DNA.
DR EMBL; AF149924; AAF03365.1; -; Genomic_DNA.
DR RefSeq; WP_011277552.1; NC_007181.1.
DR AlphaFoldDB; Q9V2T4; -.
DR SMR; Q9V2T4; -.
DR STRING; 330779.Saci_0666; -.
DR EnsemblBacteria; AAY80050; AAY80050; Saci_0666.
DR GeneID; 3473237; -.
DR KEGG; sai:Saci_0666; -.
DR PATRIC; fig|330779.12.peg.636; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR OMA; HPAANMI; -.
DR Proteomes; UP000001018; Chromosome.
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; IEA:InterPro.
DR CDD; cd03343; cpn60; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
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 InterPro; IPR012714; Thermosome_arc.
DR PANTHER; PTHR11353; PTHR11353; 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; TIGR02339; thermosome_arch; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT CHAIN 1..553
FT /note="Thermosome subunit beta"
FT /id="PRO_0000128400"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60121 MW; 64FBEFEBC2A7471F CRC64;
MSATATVATT PEGIPVIILK EGSSRTYGKE ALRINIAAVK AVEEALKTTY GPRGMDKMLV
DSLGDITITN DGATILDKMD LQHPAAKLLV QIAKGQDEET ADGTKTAVIF SGELVKKAEE
LLYKEIHPTI IVSGYKKAEE MAIKTIEEIS TKVSVNDTEI LRKVALTSLS SKAVAGAREH
LADIVVKAIT QVAELRGDKW YVDLDNVQIV KKHGGSINDT QIVYGIIVDK EVVHPGMPKR
VENAKIALLD ASLEVEKPEL DAEIRINDPT QMKKFLDEEE NILKEKVDKI AQTGANVVIC
QKGIDEVAQH YLAKKGILAV RRAKKSDLEK LARATGGRVV SNIDELTSQD LGYATLVEER
KIGEDKMVFI EGAKNPKAVS ILIRGGLERV VDETERALRD ALGTVADVVR DGRAIAGGGA
VETEIAKRLR KYAPQVGGKE QLAIEAYANA LESLVMILIE NGGFDPIELL VKLRSAHENE
TNKWHGINVY TGQIQDMWSL GVIEPAVVKM NAIKAATEAS TLILRIDDLI SAGKKSEGKT
GEKKESEKGK EED