THSA_THEKO
ID THSA_THEKO Reviewed; 548 AA.
AC P61111; O24729; Q9Y8I3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Thermosome subunit alpha;
DE AltName: Full=Chaperonin subunit alpha;
DE AltName: Full=Thermosome subunit 1;
GN Name=thsA; Synonyms=cpkA; OrderedLocusNames=TK0678;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10103287; DOI=10.1128/aem.65.4.1801-1805.1999;
RA Izumi M., Fujiwara S., Takagi M., Kanaya S., Imanaka T.;
RT "Isolation and characterization of a second subunit of molecular chaperonin
RT from Pyrococcus kodakaraensis KOD1: analysis of an ATPase-deficient mutant
RT enzyme.";
RL Appl. Environ. Microbiol. 65:1801-1805(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AB018432; BAA76952.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD84867.1; -; Genomic_DNA.
DR PIR; T43915; T43915.
DR RefSeq; WP_011249629.1; NC_006624.1.
DR PDB; 1Q3R; X-ray; 2.90 A; A/B/C/D=1-548.
DR PDBsum; 1Q3R; -.
DR AlphaFoldDB; P61111; -.
DR SMR; P61111; -.
DR STRING; 69014.TK0678; -.
DR EnsemblBacteria; BAD84867; BAD84867; TK0678.
DR GeneID; 3234606; -.
DR KEGG; tko:TK0678; -.
DR PATRIC; fig|69014.16.peg.659; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR InParanoid; P61111; -.
DR OMA; HRKGNTW; -.
DR OrthoDB; 11742at2157; -.
DR PhylomeDB; P61111; -.
DR BRENDA; 3.6.4.B10; 5246.
DR Proteomes; UP000000536; 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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..548
FT /note="Thermosome subunit alpha"
FT /id="PRO_0000128397"
FT REGION 527..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 232..242
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 262..285
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 381..403
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 459..473
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1Q3R"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:1Q3R"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:1Q3R"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:1Q3R"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:1Q3R"
SQ SEQUENCE 548 AA; 59170 MW; D7B4F3889E02A88A CRC64;
MAQLSGQPVV ILPEGTQRYV GRDAQRLNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
VTNDGATILD KIDLQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLRK AEELLDQNIH
PSIIIKGYAL AAEKAQEILD EIAIRVDPDD EETLLKIAAT SITGKNAESH KELLAKLAVE
AVKQVAEKKD GKYVVDLDNI KFEKKAGEGV EESELVRGVV IDKEVVHPRM PKRVENAKIA
LINEALEVKK TETDAKINIT SPDQLMSFLE QEEKMLKDMV DHIAQTGANV VFVQKGIDDL
AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVKDLT PEDLGYAEVV EERKLAGENM
IFVEGCKNPK AVTILIRGGT EHVIDEVERA LEDAVKVVKD VMEDGAVLPA GGAPEIELAI
RLDEYAKQVG GKEALAIENF ADALKIIPKT LAENAGLDTV EMLVKVISEH KNRGLGIGID
VFEGKPADML EKGIIEPLRV KKQAIKSASE AAIMILRIDD VIAAKATKPE GGQGGGMPGG
MGGMDMGM
