THSA_THEK1
ID THSA_THEK1 Reviewed; 548 AA.
AC P61112; O24729; Q9Y8I3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Thermosome subunit alpha;
DE AltName: Full=Chaperonin subunit alpha;
DE AltName: Full=Thermosome subunit 1;
GN Name=thsA;
OS Thermococcus sp. (strain JCM 11816 / KS-1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus; unclassified Thermococcus.
OX NCBI_TaxID=1295125;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9356252; DOI=10.1006/jmbi.1997.1337;
RA Yoshida T., Yohda M., Iida T., Maruyama T., Taguchi H., Yazaki K., Ohta T.,
RA Odaka M., Endo I., Kagawa Y.;
RT "Structural and functional characterization of homo-oligomeric complexes of
RT alpha and beta chaperonin subunits from the hyperthermophilic archaeum
RT Thermococcus strain KS-1.";
RL J. Mol. Biol. 273:635-645(1997).
RN [2]
RP SEQUENCE REVISION TO 58.
RA Yohda M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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; AB001080; BAA22207.2; -; Genomic_DNA.
DR PDB; 1Q2V; X-ray; 2.40 A; A/B/C/D=1-548.
DR PDB; 1Q3Q; X-ray; 2.30 A; A/B/C/D=1-548.
DR PDB; 1Q3R; X-ray; 2.90 A; A/B/C/D=1-548.
DR PDB; 1Q3S; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-548.
DR PDBsum; 1Q2V; -.
DR PDBsum; 1Q3Q; -.
DR PDBsum; 1Q3R; -.
DR PDBsum; 1Q3S; -.
DR AlphaFoldDB; P61112; -.
DR SMR; P61112; -.
DR BRENDA; 3.6.4.B10; 6304.
DR BRENDA; 5.6.1.7; 12506.
DR EvolutionaryTrace; P61112; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding.
FT CHAIN 1..548
FT /note="Thermosome subunit alpha"
FT /id="PRO_0000128398"
FT REGION 527..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 232..242
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 262..285
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 381..403
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 459..473
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:1Q3Q"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:1Q3Q"
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
