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Protein

ATP synthase subunit alpha

Gene

atpA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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
Sitei373 – 3731Required for activity

Regions

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

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

BioCyciEcoCyc:ATPA-MONOMER.
ECOL316407:JW3712-MONOMER.
MetaCyc:ATPA-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

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
Synonyms:papA, uncA
Ordered Locus Names:b3734, JW3712
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10098. atpA.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi175 – 1751K → E: Reduced activity and reduced ATP-binding. 1 Publication
Mutagenesisi175 – 1751K → I: Reduced activity and loss of ATP-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513ATP synthase subunit alphaPRO_0000144325Add
BLAST

Proteomic databases

EPDiP0ABB0.
PaxDbiP0ABB0.
PRIDEiP0ABB0.

2D gel databases

SWISS-2DPAGEP0ABB0.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
atpDP0ABB410EBI-368707,EBI-368783

Protein-protein interaction databases

DIPiDIP-31845N.
IntActiP0ABB0. 28 interactions.
MINTiMINT-1251537.
STRINGi511145.b3734.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358Combined sources
Beta strandi38 – 436Combined sources
Beta strandi52 – 554Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 668Combined sources
Beta strandi71 – 777Combined sources
Beta strandi87 – 893Combined sources
Beta strandi94 – 985Combined sources
Helixi101 – 1033Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi136 – 1383Combined sources
Helixi151 – 1566Combined sources
Beta strandi166 – 1749Combined sources
Helixi175 – 18410Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi192 – 1998Combined sources
Helixi202 – 21514Combined sources
Beta strandi221 – 2266Combined sources
Helixi232 – 25120Combined sources
Beta strandi255 – 2617Combined sources
Helixi263 – 27614Combined sources
Helixi290 – 2989Combined sources
Beta strandi302 – 3043Combined sources
Helixi306 – 3138Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 3353Combined sources
Helixi340 – 3489Combined sources
Beta strandi349 – 3557Combined sources
Helixi357 – 3604Combined sources
Turni370 – 3723Combined sources
Beta strandi374 – 3774Combined sources
Helixi378 – 3814Combined sources
Helixi384 – 40724Combined sources
Helixi415 – 43016Combined sources
Helixi443 – 45210Combined sources
Turni455 – 4595Combined sources
Helixi462 – 47514Combined sources
Helixi477 – 4793Combined sources
Helixi481 – 4899Combined sources
Helixi494 – 50714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40A/B/C1-513[»]
3OAAX-ray3.26A/B/C/I/J/K/Q/R/S/Y/Z/a1-513[»]
ProteinModelPortaliP0ABB0.
SMRiP0ABB0. Positions 24-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABB0.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CDG. Bacteria.
COG0056. LUCA.
HOGENOMiHOG000130111.
InParanoidiP0ABB0.
KOiK02111.
OMAiPVFCIYV.
PhylomeDBiP0ABB0.

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]
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]
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.

P0ABB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG
60 70 80 90 100
EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG
110 120 130 140 150
RGLLGRVVNT LGAPIDGKGP LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY
160 170 180 190 200
KAVDSMIPIG RGQRELIIGD RQTGKTALAI DAIINQRDSG IKCIYVAIGQ
210 220 230 240 250
KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY AGCAMGEYFR
260 270 280 290 300
DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
310 320 330 340 350
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD
360 370 380 390 400
GQIFLETNLF NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY
410 420 430 440 450
RELAAFSQFA SDLDDATRKQ LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA
460 470 480 490 500
AERGYLADVE LSKIGSFEAA LLAYVDRDHA PLMQEINQTG GYNDEIEGKL
510
KGILDSFKAT QSW
Length:513
Mass (Da):55,222
Last modified:November 8, 2005 - v1
Checksum:iDD1F3859375E9103
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911T → I in AAA83873 (PubMed:6301339).Curated
Sequence conflicti239 – 2446PYAGCA → RMPVAL in CAA25780 (PubMed:6301339).Curated
Sequence conflicti239 – 2446PYAGCA → RMPVAL in AAA24735 (PubMed:6301339).Curated
Sequence conflicti300 – 3023RAA → MLQ in CAA23519 (PubMed:6272228).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01631 Genomic DNA. Translation: CAA25780.1. Sequence problems.
J01594 Genomic DNA. Translation: AAA24735.1. Sequence problems.
V00265 Genomic DNA. Translation: CAA23519.1. Sequence problems.
V00312 Genomic DNA. Translation: CAA23596.1. Sequence problems.
M12212 Unassigned DNA. Translation: AAA20045.1.
M25464 Genomic DNA. Translation: AAA83873.1.
L10328 Genomic DNA. Translation: AAA62086.1.
U00096 Genomic DNA. Translation: AAC76757.1.
AP009048 Genomic DNA. Translation: BAE77554.1.
V00266 Genomic DNA. Translation: CAA23525.1.
PIRiG65176. PWECA.
RefSeqiNP_418190.1. NC_000913.3.
WP_001176745.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76757; AAC76757; b3734.
BAE77554; BAE77554; BAE77554.
GeneIDi948242.
KEGGiecj:JW3712.
eco:b3734.
PATRICi32122965. VBIEscCol129921_3858.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01631 Genomic DNA. Translation: CAA25780.1. Sequence problems.
J01594 Genomic DNA. Translation: AAA24735.1. Sequence problems.
V00265 Genomic DNA. Translation: CAA23519.1. Sequence problems.
V00312 Genomic DNA. Translation: CAA23596.1. Sequence problems.
M12212 Unassigned DNA. Translation: AAA20045.1.
M25464 Genomic DNA. Translation: AAA83873.1.
L10328 Genomic DNA. Translation: AAA62086.1.
U00096 Genomic DNA. Translation: AAC76757.1.
AP009048 Genomic DNA. Translation: BAE77554.1.
V00266 Genomic DNA. Translation: CAA23525.1.
PIRiG65176. PWECA.
RefSeqiNP_418190.1. NC_000913.3.
WP_001176745.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40A/B/C1-513[»]
3OAAX-ray3.26A/B/C/I/J/K/Q/R/S/Y/Z/a1-513[»]
ProteinModelPortaliP0ABB0.
SMRiP0ABB0. Positions 24-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-31845N.
IntActiP0ABB0. 28 interactions.
MINTiMINT-1251537.
STRINGi511145.b3734.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGEP0ABB0.

Proteomic databases

EPDiP0ABB0.
PaxDbiP0ABB0.
PRIDEiP0ABB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76757; AAC76757; b3734.
BAE77554; BAE77554; BAE77554.
GeneIDi948242.
KEGGiecj:JW3712.
eco:b3734.
PATRICi32122965. VBIEscCol129921_3858.

Organism-specific databases

EchoBASEiEB0096.
EcoGeneiEG10098. atpA.

Phylogenomic databases

eggNOGiENOG4105CDG. Bacteria.
COG0056. LUCA.
HOGENOMiHOG000130111.
InParanoidiP0ABB0.
KOiK02111.
OMAiPVFCIYV.
PhylomeDBiP0ABB0.

Enzyme and pathway databases

BioCyciEcoCyc:ATPA-MONOMER.
ECOL316407:JW3712-MONOMER.
MetaCyc:ATPA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABB0.
PROiP0ABB0.

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]
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]
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_ECOLI
AccessioniPrimary (citable) accession number: P0ABB0
Secondary accession number(s): P00822, Q2M852, Q47249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 8, 2005
Last modified: September 7, 2016
This is version 104 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.