THSA_THEAC
ID THSA_THEAC Reviewed; 545 AA.
AC P48424;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Thermosome subunit alpha;
DE AltName: Full=Chaperonin subunit alpha;
DE AltName: Full=Thermosome subunit 1;
GN Name=thsA; OrderedLocusNames=Ta0980;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 88-97 AND
RP 427-436.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=7794526; DOI=10.1515/bchm3.1995.376.2.119;
RA Waldmann T., Lupas A.N., Kellermann J., Peters J., Baumeister W.;
RT "Primary structure of the thermosome from Thermoplasma acidophilum.";
RL Biol. Chem. Hoppe-Seyler 376:119-126(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP PROTEIN SEQUENCE OF 80-114 AND 420-444.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=7867646; DOI=10.1111/j.1432-1033.1995.tb20210.x;
RA Waldmann T., Nimmesgern E., Nitsch M., Peters J., Pfeifer G., Mueller S.,
RA Kellermann J., Engel A., Hartl F.-U., Baumeister W.;
RT "The thermosome of Thermoplasma acidophilum and its relationship to the
RT eukaryotic chaperonin TRiC.";
RL Eur. J. Biochem. 227:848-856(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 213-364.
RX PubMed=9346243; DOI=10.1016/s0092-8674(00)80408-0;
RA Klumpp M., Baumeister W., Essen L.-O.;
RT "Structure of the substrate binding domain of the thermosome, an archaeal
RT group II chaperonin.";
RL Cell 91:263-270(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9546398; DOI=10.1016/s0092-8674(00)81152-6;
RA Ditzel L., Loewe J., Stock D., Stetter K.-O., Huber H., Huber R.,
RA Steinbacher S.;
RT "Crystal structure of the thermosome, the archaeal chaperonin and homolog
RT of CCT.";
RL Cell 93:125-138(1998).
CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC and has a weak ATPase activity.
CC -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC rings.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC12109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z46649; CAA86610.1; -; Genomic_DNA.
DR EMBL; AL445066; CAC12109.1; ALT_INIT; Genomic_DNA.
DR PIR; S53816; S53816.
DR RefSeq; WP_048161900.1; NC_002578.1.
DR PDB; 1A6D; X-ray; 2.60 A; A=1-545.
DR PDB; 1A6E; X-ray; 3.20 A; A=1-545.
DR PDB; 1ASS; X-ray; 2.30 A; A=214-365.
DR PDB; 1ASX; X-ray; 2.80 A; A=214-365.
DR PDBsum; 1A6D; -.
DR PDBsum; 1A6E; -.
DR PDBsum; 1ASS; -.
DR PDBsum; 1ASX; -.
DR AlphaFoldDB; P48424; -.
DR BMRB; P48424; -.
DR SMR; P48424; -.
DR MINT; P48424; -.
DR STRING; 273075.Ta0980; -.
DR PRIDE; P48424; -.
DR EnsemblBacteria; CAC12109; CAC12109; CAC12109.
DR GeneID; 1456505; -.
DR KEGG; tac:Ta0980; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR OMA; HRKGNTW; -.
DR OrthoDB; 11742at2157; -.
DR BRENDA; 3.6.4.B10; 6324.
DR BRENDA; 5.6.1.7; 6324.
DR EvolutionaryTrace; P48424; -.
DR Proteomes; UP000001024; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..545
FT /note="Thermosome subunit alpha"
FT /id="PRO_0000128409"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 20..39
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 95..116
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 120..141
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 229..241
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 262..282
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1ASS"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 342..352
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:1ASS"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 381..401
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 410..424
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 428..441
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 443..452
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 495..513
FT /evidence="ECO:0007829|PDB:1A6D"
SQ SEQUENCE 545 AA; 58281 MW; 0E0B3241DF62C63C CRC64;
MMTGQVPILV LKEGTQREQG KNAQRNNIEA AKAIADAVRT TLGPKGMDKM LVDSIGDIII
SNDGATILKE MDVEHPTAKM IVEVSKAQDT AVGDGTTTAV VLSGELLKQA ETLLDQGVHP
TVISNGYRLA VNEARKIIDE IAEKSTDDAT LRKIALTALS GKNTGLSNDF LADLVVKAVN
AVAEVRDGKT IVDTANIKVD KKNGGSVNDT QFISGIVIDK EKVHSKMPDV VKNAKIALID
SALEIKKTEI EAKVQISDPS KIQDFLNQET NTFKQMVEKI KKSGANVVLC QKGIDDVAQH
YLAKEGIYAV RRVKKSDMEK LAKATGAKIV TDLDDLTPSV LGEAETVEER KIGDDRMTFV
MGCKNPKAVS ILIRGGTDHV VSEVERALND AIRVVAITKE DGKFLWGGGA VEAELAMRLA
KYANSVGGRE QLAIEAFAKA LEIIPRTLAE NAGIDPINTL IKLKAEHEKG RISVGVDLDN
NGVGDMKAKG VVDPLRVKTH ALESAVEVAT MILRIDDVIA SKKSTPPSGQ GGQGQGMPGG
GMPEY
