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Protein

ATP synthase subunit alpha

Gene

atpA

Organism
Bacillus sp. (strain PS3)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei362Required for activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 176ATPUniRule 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

Enzyme and pathway databases

SABIO-RKP09219.

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
OrganismiBacillus sp. (strain PS3)
Taxonomic identifieri2334 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001443161 – 502ATP synthase subunit alphaAdd BLAST502

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 annotation1 Publication

Protein-protein interaction databases

DIPiDIP-6214N.
MINTiMINT-1526861.

Structurei

Secondary structure

1502
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 27Combined sources3
Beta strandi28 – 35Combined sources8
Beta strandi38 – 43Combined sources6
Beta strandi51 – 55Combined sources5
Beta strandi60 – 67Combined sources8
Beta strandi70 – 77Combined sources8
Beta strandi87 – 98Combined sources12
Turni102 – 105Combined sources4
Beta strandi116 – 118Combined sources3
Beta strandi126 – 130Combined sources5
Beta strandi136 – 139Combined sources4
Beta strandi144 – 146Combined sources3
Helixi151 – 156Combined sources6
Beta strandi166 – 169Combined sources4
Helixi175 – 184Combined sources10
Turni185 – 190Combined sources6
Beta strandi192 – 199Combined sources8
Helixi202 – 214Combined sources13
Beta strandi220 – 226Combined sources7
Helixi232 – 250Combined sources19
Turni251 – 253Combined sources3
Beta strandi255 – 261Combined sources7
Helixi263 – 276Combined sources14
Helixi283 – 285Combined sources3
Helixi290 – 298Combined sources9
Helixi306 – 308Combined sources3
Beta strandi312 – 320Combined sources9
Helixi322 – 324Combined sources3
Helixi329 – 335Combined sources7
Beta strandi338 – 344Combined sources7
Helixi346 – 352Combined sources7
Turni359 – 361Combined sources3
Beta strandi363 – 366Combined sources4
Beta strandi368 – 371Combined sources4
Helixi373 – 392Combined sources20
Helixi404 – 420Combined sources17
Helixi430 – 439Combined sources10
Turni440 – 447Combined sources8
Helixi450 – 452Combined sources3
Helixi453 – 466Combined sources14
Helixi467 – 470Combined sources4
Helixi472 – 478Combined sources7
Helixi483 – 497Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20B1-502[»]
ProteinModelPortaliP09219.
SMRiP09219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09219.

Family & Domainsi

Sequence similaritiesi

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

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.

P09219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIRAEEISA LIKQQIENYE SQIQVSDVGT VIQVGDGIAR AHGLDNVMSG
60 70 80 90 100
EAVEFANAVM GMALNLEENN VGIVILGPYT GIKEGDEVRR TGRIMEVPVG
110 120 130 140 150
ETLIGRVVNP LGQPVDGLGP VETTETRPIE SRAPGVMDRR SVHEPLQTGI
160 170 180 190 200
KAIDALVPIG RGQRELIIGD RQTGKTSVAI DTIINQKDQN MICIYVAIGQ
210 220 230 240 250
KESTVATVVE TLAKHGAPDY TIVVTASASQ PAPLLFLAPY AGVAMGEYFM
260 270 280 290 300
IMGKHVLVVI DDLSKQAAAY RQLSLLLRRP PGREAYPGDI FYLHSRLLER
310 320 330 340 350
AAKLSDAKGG GSLTALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF
360 370 380 390 400
SGVRPAINAG LSVSRVGGAA QIKAMKKVAG TLRLDLAAYR ELEAFAQFGS
410 420 430 440 450
DLDKATQANV ARGARTVEVL KQDLHQPIPV EKQVLIIYAL TRGFLDDIPV
460 470 480 490 500
EDVRRFEKEF YLWLDQNGQH LLEHIRTTKD LPNEDDLNQA IEAFKKTFVV

SQ
Length:502
Mass (Da):54,591
Last modified:July 1, 1989 - v1
Checksum:i19B2721AD8CF8661
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07804 Genomic DNA. Translation: CAA30652.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07804 Genomic DNA. Translation: CAA30652.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20B1-502[»]
ProteinModelPortaliP09219.
SMRiP09219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6214N.
MINTiMINT-1526861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP09219.

Miscellaneous databases

EvolutionaryTraceiP09219.

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_BACP3
AccessioniPrimary (citable) accession number: P09219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 128 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, Direct protein sequencing

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.