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Protein

ATP synthase subunit alpha

Gene

atpA

Organism
Bacillus sp. (strain PS3)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei362 – 3621Required for activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1768ATPUniRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502ATP synthase subunit alphaPRO_0000144316Add
BLAST

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

1
502
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 273Combined sources
Beta strandi28 – 358Combined sources
Beta strandi38 – 436Combined sources
Beta strandi51 – 555Combined sources
Beta strandi60 – 678Combined sources
Beta strandi70 – 778Combined sources
Beta strandi87 – 9812Combined sources
Turni102 – 1054Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi144 – 1463Combined sources
Helixi151 – 1566Combined sources
Beta strandi166 – 1694Combined sources
Helixi175 – 18410Combined sources
Turni185 – 1906Combined sources
Beta strandi192 – 1998Combined sources
Helixi202 – 21413Combined sources
Beta strandi220 – 2267Combined sources
Helixi232 – 25019Combined sources
Turni251 – 2533Combined sources
Beta strandi255 – 2617Combined sources
Helixi263 – 27614Combined sources
Helixi283 – 2853Combined sources
Helixi290 – 2989Combined sources
Helixi306 – 3083Combined sources
Beta strandi312 – 3209Combined sources
Helixi322 – 3243Combined sources
Helixi329 – 3357Combined sources
Beta strandi338 – 3447Combined sources
Helixi346 – 3527Combined sources
Turni359 – 3613Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi368 – 3714Combined sources
Helixi373 – 39220Combined sources
Helixi404 – 42017Combined sources
Helixi430 – 43910Combined sources
Turni440 – 4478Combined sources
Helixi450 – 4523Combined sources
Helixi453 – 46614Combined sources
Helixi467 – 4704Combined sources
Helixi472 – 4787Combined sources
Helixi483 – 49715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20B1-502[»]
ProteinModelPortaliP09219.
SMRiP09219. Positions 21-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09219.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
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.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20B1-502[»]
ProteinModelPortaliP09219.
SMRiP09219. Positions 21-502.
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

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
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.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3."
    Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T., Otawara-Hamamoto Y., Matsuda K., Kagawa Y.
    Biochim. Biophys. Acta 933:141-155(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-42; 106-121 AND 164-174, SUBUNIT.
  2. "The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer."
    Shirakihara Y., Leslie A.G.W., Abrahams J.P., Walker J.E., Ueda T., Seikimoto Y., Kambara M., Saika K., Kagawa Y., Yoshida M.
    Structure 5:825-836(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).

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: May 11, 2016
This is version 124 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.