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Protein

ATP synthase subunit alpha

Gene

atpA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei363Required for activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi170 – 177ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alphaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit alphaUniRule annotation
F-ATPase subunit alphaUniRule annotation
Gene namesi
Name:atpAUniRule annotation
Ordered Locus Names:TM_1612
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002383871 – 503ATP synthase subunit alphaAdd BLAST503

Proteomic databases

PRIDEiQ9X1U7.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

Protein-protein interaction databases

STRINGi243274.TM1612.

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni25 – 27Combined sources3
Beta strandi28 – 35Combined sources8
Beta strandi38 – 43Combined sources6
Beta strandi51 – 55Combined sources5
Turni56 – 58Combined sources3
Beta strandi61 – 66Combined sources6
Beta strandi72 – 78Combined sources7
Beta strandi88 – 95Combined sources8
Beta strandi97 – 101Combined sources5
Helixi102 – 104Combined sources3
Beta strandi117 – 119Combined sources3
Beta strandi125 – 130Combined sources6
Helixi137 – 139Combined sources3
Beta strandi145 – 147Combined sources3
Helixi152 – 157Combined sources6
Beta strandi165 – 171Combined sources7
Helixi176 – 185Combined sources10
Turni186 – 191Combined sources6
Beta strandi192 – 200Combined sources9
Helixi203 – 215Combined sources13
Helixi218 – 221Combined sources4
Beta strandi222 – 227Combined sources6
Helixi233 – 251Combined sources19
Turni252 – 254Combined sources3
Beta strandi256 – 262Combined sources7
Helixi264 – 276Combined sources13
Helixi291 – 299Combined sources9
Beta strandi303 – 305Combined sources3
Turni307 – 310Combined sources4
Beta strandi313 – 323Combined sources11
Helixi330 – 337Combined sources8
Beta strandi339 – 345Combined sources7
Helixi347 – 352Combined sources6
Turni360 – 362Combined sources3
Helixi366 – 368Combined sources3
Turni369 – 371Combined sources3
Helixi374 – 394Combined sources21
Helixi397 – 399Combined sources3
Helixi405 – 420Combined sources16
Helixi431 – 442Combined sources12
Turni443 – 448Combined sources6
Helixi451 – 453Combined sources3
Helixi454 – 468Combined sources15
Helixi470 – 479Combined sources10
Helixi484 – 500Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R9VX-ray2.10A2-503[»]
ProteinModelPortaliQ9X1U7.
SMRiQ9X1U7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X1U7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDG. Bacteria.
COG0056. LUCA.
InParanoidiQ9X1U7.
KOiK02111.
OMAiQVVSIWA.

Family and domain databases

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X1U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRINPGEITK VLEEKIKSFE EKIDLEDTGK VIQVGDGIAR AYGLNKVMVS
60 70 80 90 100
ELVEFVETGV KGVAFNLEED NVGIIILGEY KDIKEGHTVR RLKRIIEVPV
110 120 130 140 150
GEELLGRVVN PLGEPLDGKG PINAKNFRPI EIKAPGVIYR KPVDTPLQTG
160 170 180 190 200
IKAIDSMIPI GRGQRELIIG DRQTGKTAIA IDTIINQKGQ GVYCIYVAIG
210 220 230 240 250
QKKSAIARII DKLRQYGAME YTTVVVASAS DPASLQYIAP YAGCAMGEYF
260 270 280 290 300
AYSGRDALVV YDDLSKHAVA YRQLSLLMRR PPGREAYPGD IFYLHSRLLE
310 320 330 340 350
RAVRLNDKLG GGSLTALPIV ETQANDISAY IPTNVISITD GQIYLEPGLF
360 370 380 390 400
YAGQRPAINV GLSVSRVGGS AQIKAMKQVA GMLRIDLAQY RELETFAQFA
410 420 430 440 450
TELDPATRAQ IIRGQRLMEL LKQEQYSPMP VEEQVVVLFA GVRGYLDDLP
460 470 480 490 500
VEEVRRFEKE FLRFMHEKHQ DILDDIKTKK ELTSETEEKL KKAIEEFKTT

FRV
Length:503
Mass (Da):56,062
Last modified:November 1, 1999 - v1
Checksum:i886C9736F16BF149
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36679.1.
PIRiF72231.
RefSeqiNP_229412.1. NC_000853.1.
WP_004082064.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36679; AAD36679; TM_1612.
GeneIDi897935.
KEGGitma:TM1612.
PATRICi23938198. VBITheMar51294_1631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36679.1.
PIRiF72231.
RefSeqiNP_229412.1. NC_000853.1.
WP_004082064.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R9VX-ray2.10A2-503[»]
ProteinModelPortaliQ9X1U7.
SMRiQ9X1U7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1612.

Proteomic databases

PRIDEiQ9X1U7.

Protocols and materials databases

DNASUi897935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36679; AAD36679; TM_1612.
GeneIDi897935.
KEGGitma:TM1612.
PATRICi23938198. VBITheMar51294_1631.

Phylogenomic databases

eggNOGiENOG4105CDG. Bacteria.
COG0056. LUCA.
InParanoidiQ9X1U7.
KOiK02111.
OMAiQVVSIWA.

Miscellaneous databases

EvolutionaryTraceiQ9X1U7.

Family and domain databases

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATPA_THEMA
AccessioniPrimary (citable) accession number: Q9X1U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 119 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, 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.