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Protein

Thermosome subunit alpha

Gene

thsA

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.9. 6324.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermosome subunit alpha
Alternative name(s):
Chaperonin subunit alpha
Thermosome subunit 1
Gene namesi
Name:thsA
Ordered Locus Names:Ta0980
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545Thermosome subunit alphaPRO_0000128409Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP48424.

Interactioni

Subunit structurei

Forms a Heterooligomeric complex of two stacked eight-membered rings.

Protein-protein interaction databases

MINTiMINT-1534030.
STRINGi273075.Ta0980.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3920Combined sources
Beta strandi48 – 525Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 614Combined sources
Helixi64 – 707Combined sources
Helixi76 – 827Combined sources
Helixi83 – 864Combined sources
Turni88 – 903Combined sources
Helixi95 – 11622Combined sources
Helixi120 – 14122Combined sources
Helixi148 – 15811Combined sources
Turni159 – 1613Combined sources
Helixi168 – 18215Combined sources
Beta strandi184 – 1918Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi229 – 24113Combined sources
Helixi247 – 2559Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 28221Combined sources
Beta strandi286 – 2927Combined sources
Helixi296 – 3049Combined sources
Beta strandi308 – 3103Combined sources
Helixi315 – 32511Combined sources
Beta strandi330 – 3323Combined sources
Helixi333 – 3353Combined sources
Helixi338 – 3403Combined sources
Beta strandi342 – 35211Combined sources
Beta strandi355 – 3628Combined sources
Beta strandi369 – 3735Combined sources
Beta strandi376 – 3783Combined sources
Helixi381 – 40121Combined sources
Beta strandi403 – 4064Combined sources
Turni407 – 4093Combined sources
Helixi410 – 42415Combined sources
Helixi428 – 44114Combined sources
Helixi443 – 45210Combined sources
Helixi456 – 46813Combined sources
Beta strandi474 – 4774Combined sources
Turni478 – 4814Combined sources
Beta strandi482 – 4854Combined sources
Helixi486 – 4894Combined sources
Beta strandi492 – 4943Combined sources
Helixi495 – 51319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6DX-ray2.60A1-545[»]
1A6EX-ray3.20A1-545[»]
1ASSX-ray2.30A214-365[»]
1ASXX-ray2.80A214-365[»]
ProteinModelPortaliP48424.
SMRiP48424. Positions 17-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48424.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiarCOG01257. Archaea.
COG0459. LUCA.
HOGENOMiHOG000226730.
OMAiHYLAQEG.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
IPR012714. Thermosome_arc.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02339. thermosome_arch. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTGQVPILV LKEGTQREQG KNAQRNNIEA AKAIADAVRT TLGPKGMDKM
60 70 80 90 100
LVDSIGDIII SNDGATILKE MDVEHPTAKM IVEVSKAQDT AVGDGTTTAV
110 120 130 140 150
VLSGELLKQA ETLLDQGVHP TVISNGYRLA VNEARKIIDE IAEKSTDDAT
160 170 180 190 200
LRKIALTALS GKNTGLSNDF LADLVVKAVN AVAEVRDGKT IVDTANIKVD
210 220 230 240 250
KKNGGSVNDT QFISGIVIDK EKVHSKMPDV VKNAKIALID SALEIKKTEI
260 270 280 290 300
EAKVQISDPS KIQDFLNQET NTFKQMVEKI KKSGANVVLC QKGIDDVAQH
310 320 330 340 350
YLAKEGIYAV RRVKKSDMEK LAKATGAKIV TDLDDLTPSV LGEAETVEER
360 370 380 390 400
KIGDDRMTFV MGCKNPKAVS ILIRGGTDHV VSEVERALND AIRVVAITKE
410 420 430 440 450
DGKFLWGGGA VEAELAMRLA KYANSVGGRE QLAIEAFAKA LEIIPRTLAE
460 470 480 490 500
NAGIDPINTL IKLKAEHEKG RISVGVDLDN NGVGDMKAKG VVDPLRVKTH
510 520 530 540
ALESAVEVAT MILRIDDVIA SKKSTPPSGQ GGQGQGMPGG GMPEY
Length:545
Mass (Da):58,281
Last modified:February 1, 1996 - v1
Checksum:i0E0B3241DF62C63C
GO

Sequence cautioni

The sequence CAC12109.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46649 Genomic DNA. Translation: CAA86610.1.
AL445066 Genomic DNA. Translation: CAC12109.1. Different initiation.
PIRiS53816.
RefSeqiWP_048161900.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC12109; CAC12109; CAC12109.
GeneIDi1456505.
KEGGitac:Ta0980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46649 Genomic DNA. Translation: CAA86610.1.
AL445066 Genomic DNA. Translation: CAC12109.1. Different initiation.
PIRiS53816.
RefSeqiWP_048161900.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6DX-ray2.60A1-545[»]
1A6EX-ray3.20A1-545[»]
1ASSX-ray2.30A214-365[»]
1ASXX-ray2.80A214-365[»]
ProteinModelPortaliP48424.
SMRiP48424. Positions 17-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1534030.
STRINGi273075.Ta0980.

Proteomic databases

PRIDEiP48424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC12109; CAC12109; CAC12109.
GeneIDi1456505.
KEGGitac:Ta0980.

Phylogenomic databases

eggNOGiarCOG01257. Archaea.
COG0459. LUCA.
HOGENOMiHOG000226730.
OMAiHYLAQEG.

Enzyme and pathway databases

BRENDAi3.6.4.9. 6324.

Miscellaneous databases

EvolutionaryTraceiP48424.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
IPR012714. Thermosome_arc.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02339. thermosome_arch. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the thermosome from Thermoplasma acidophilum."
    Waldmann T., Lupas A.N., Kellermann J., Peters J., Baumeister W.
    Biol. Chem. Hoppe-Seyler 376:119-126(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 88-97 AND 427-436.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  2. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  3. "The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC."
    Waldmann T., Nimmesgern E., Nitsch M., Peters J., Pfeifer G., Mueller S., Kellermann J., Engel A., Hartl F.-U., Baumeister W.
    Eur. J. Biochem. 227:848-856(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-114 AND 420-444.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  4. "Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin."
    Klumpp M., Baumeister W., Essen L.-O.
    Cell 91:263-270(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 213-364.
  5. "Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT."
    Ditzel L., Loewe J., Stock D., Stetter K.-O., Huber H., Huber R., Steinbacher S.
    Cell 93:125-138(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiTHSA_THEAC
AccessioniPrimary (citable) accession number: P48424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.