Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit alpha, chloroplastic

Gene

atpA

Organism
Spinacia oleracea (Spinach)
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
Sitei363 – 3631Required for activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 1778ATPUniRule 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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, chloroplasticUniRule 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
Encoded oniPlastid; Chloroplast
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

  • Plastidchloroplast thylakoid membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(1), Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507ATP synthase subunit alpha, chloroplasticPRO_0000144392Add
BLAST

Proteomic databases

PRIDEiP06450.

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 four main subunits: a, b, b' and c.UniRule annotation

Protein-protein interaction databases

MINTiMINT-147559.

Structurei

Secondary structure

1
507
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 283Combined sources
Beta strandi29 – 324Combined sources
Beta strandi37 – 448Combined sources
Beta strandi54 – 563Combined sources
Beta strandi61 – 677Combined sources
Beta strandi69 – 768Combined sources
Helixi80 – 823Combined sources
Beta strandi88 – 903Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi137 – 1404Combined sources
Turni152 – 1576Combined sources
Beta strandi167 – 1759Combined sources
Helixi176 – 18510Combined sources
Turni189 – 1913Combined sources
Beta strandi193 – 2008Combined sources
Helixi203 – 21210Combined sources
Turni213 – 2175Combined sources
Helixi218 – 2203Combined sources
Beta strandi221 – 2277Combined sources
Beta strandi229 – 2313Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 25215Combined sources
Beta strandi256 – 2627Combined sources
Helixi264 – 27714Combined sources
Helixi284 – 2863Combined sources
Turni293 – 2986Combined sources
Helixi299 – 3013Combined sources
Beta strandi303 – 3053Combined sources
Turni307 – 3104Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi319 – 3213Combined sources
Helixi330 – 3367Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi347 – 3537Combined sources
Turni360 – 3623Combined sources
Helixi368 – 3714Combined sources
Helixi374 – 39320Combined sources
Turni394 – 3963Combined sources
Helixi397 – 3993Combined sources
Helixi405 – 42117Combined sources
Helixi431 – 44212Combined sources
Beta strandi445 – 4495Combined sources
Helixi451 – 46717Combined sources
Helixi470 – 47910Combined sources
Helixi484 – 49815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20A1-507[»]
1KMHX-ray3.40A1-507[»]
ProteinModelPortaliP06450.
SMRiP06450. Positions 25-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06450.

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.
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.
IPR033732. F1_ATPase_alpha.
IPR027417. P-loop_NTPase.
[Graphical view]
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.

P06450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIRADEIS KIIRERIEGY NREVKVVNTG TVLQVGDGIA RIHGLDEVMA
60 70 80 90 100
GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV
110 120 130 140 150
SEAYLGRVIN ALAKPIDGRG EITASESRLI ESPAPGIMSR RSVYEPLQTG
160 170 180 190 200
LIAIDAMIPV GRGQRELIIG DRQTGKTAVA TDTILNQQGQ NVICVYVAIG
210 220 230 240 250
QKASSVAQVV TNFQERGAME YTIVVAETAD SPATLQYLAP YTGAALAEYF
260 270 280 290 300
MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
310 320 330 340 350
RAAKLSSLLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF
360 370 380 390 400
NAGIRPAINV GISVSRVGSA AQIKAMKKVA GKLKLELAQF AELEAFAQFA
410 420 430 440 450
SDLDKATQNQ LARGQRLREL LKQPQSAPLT VEEQVMTIYT GTNGYLDSLE
460 470 480 490 500
LDQVRKYLVE LRTYVKTNKP EFQEIISSTK TFTEEAEALL KEAIQEQMER

FLLQEQA
Length:507
Mass (Da):55,451
Last modified:August 1, 1988 - v1
Checksum:i97F0C73CE8B18417
GO

Sequence cautioni

The sequence CAB88710 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03775 Genomic DNA. Translation: CAA27403.1.
AJ400848 Genomic DNA. Translation: CAB88710.1. Different initiation.
PIRiS00584. PWSPA.
RefSeqiNP_054917.2. NC_002202.1.

Genome annotation databases

GeneIDi2715575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03775 Genomic DNA. Translation: CAA27403.1.
AJ400848 Genomic DNA. Translation: CAB88710.1. Different initiation.
PIRiS00584. PWSPA.
RefSeqiNP_054917.2. NC_002202.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20A1-507[»]
1KMHX-ray3.40A1-507[»]
ProteinModelPortaliP06450.
SMRiP06450. Positions 25-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-147559.

Chemistry

ChEMBLiCHEMBL2366567.

Proteomic databases

PRIDEiP06450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2715575.

Miscellaneous databases

EvolutionaryTraceiP06450.
PROiP06450.

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.
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.
IPR033732. F1_ATPase_alpha.
IPR027417. P-loop_NTPase.
[Graphical view]
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...

Entry informationi

Entry nameiATPA_SPIOL
AccessioniPrimary (citable) accession number: P06450
Secondary accession number(s): Q9LD04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1988
Last modified: September 7, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.