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P0ABB0 (ATPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha

EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha
F-ATPase subunit alpha
Gene names
Name:atpA
Synonyms:papA, uncA
Ordered Locus Names:b3734, JW3712
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. HAMAP-Rule MF_01346

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01346

Subunit structure

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 By similarity. Ref.14

Subcellular location

Cell inner membrane; Peripheral membrane protein Ref.14.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

atpDP0ABB410EBI-368707,EBI-368783

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513ATP synthase subunit alpha HAMAP-Rule MF_01346
PRO_0000144325

Regions

Nucleotide binding169 – 1768ATP Probable

Sites

Site3731Required for activity

Experimental info

Mutagenesis1751K → E: Reduced activity and reduced ATP-binding. Ref.12
Mutagenesis1751K → I: Reduced activity and loss of ATP-binding. Ref.12
Sequence conflict911T → I in AAA83873. Ref.4
Sequence conflict239 – 2446PYAGCA → RMPVAL in CAA25780. Ref.4
Sequence conflict239 – 2446PYAGCA → RMPVAL in AAA24735. Ref.4
Sequence conflict300 – 3023RAA → MLQ in CAA23519. Ref.2

Secondary structure

................................................................................ 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABB0 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DD1F3859375E9103

FASTA51355,222
        10         20         30         40         50         60 
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG EMISLPGNRY 

        70         80         90        100        110        120 
AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG RGLLGRVVNT LGAPIDGKGP 

       130        140        150        160        170        180 
LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY KAVDSMIPIG RGQRELIIGD RQTGKTALAI 

       190        200        210        220        230        240 
DAIINQRDSG IKCIYVAIGQ KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY 

       250        260        270        280        290        300 
AGCAMGEYFR DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER 

       310        320        330        340        350        360 
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETNLF 

       370        380        390        400        410        420 
NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY RELAAFSQFA SDLDDATRKQ 

       430        440        450        460        470        480 
LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA AERGYLADVE LSKIGSFEAA LLAYVDRDHA 

       490        500        510 
PLMQEINQTG GYNDEIEGKL KGILDSFKAT QSW 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
Walker J.E., Gay N.J., Saraste M., Eberle A.N.
Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The atp operon: nucleotide sequence of the region encoding the alpha-subunit of Escherichia coli ATP-synthase."
Gay N.J., Walker J.E.
Nucleic Acids Res. 9:2187-2194(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli."
Kanazawa H., Kayano T., Mabuchi K., Futai M.
Biochem. Biophys. Res. Commun. 103:604-612(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
Kanazawa H., Futai M.
Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli."
Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.
Mol. Gen. Genet. 184:33-39(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
[9]"Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence."
Slan-Lotter H., Clarke D.M., Bragg P.D.
FEBS Lett. 197:121-124(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 239-244.
[10]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-8.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[12]"Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase."
Rao R., Pagan J., Senior A.E.
J. Biol. Chem. 263:15957-15963(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-175.
[13]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[14]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[15]"Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by X-ray crystallography."
Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.
Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) OF AN ALPHA(3)/BETA (3)/GAMMA/EPSILON COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPWECA. G65176.
RefSeqNP_418190.1. NC_000913.3.
YP_491695.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40A/B/C1-513[»]
3OAAX-ray3.26A/B/C/I/J/K/Q/R/S/Y/Z/a1-513[»]
ProteinModelPortalP0ABB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31845N.
IntActP0ABB0. 28 interactions.
MINTMINT-1251537.
STRING511145.b3734.

Protein family/group databases

TCDB3.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

PaxDbP0ABB0.
PRIDEP0ABB0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76757; AAC76757; b3734.
BAE77554; BAE77554; BAE77554.
GeneID12932824.
948242.
KEGGecj:Y75_p3434.
eco:b3734.
PATRIC32122965. VBIEscCol129921_3858.

Organism-specific databases

EchoBASEEB0096.
EcoGeneEG10098. atpA.

Phylogenomic databases

eggNOGCOG0056.
HOGENOMHOG000130111.
KOK02111.
OMANDEIKDT.
OrthoDBEOG67X1S1.
PhylomeDBP0ABB0.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0ABB0.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. 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.
IPR018538. HAS-barrel.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF09378. HAS-barrel. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABB0.
PROP0ABB0.

Entry information

Entry nameATPA_ECOLI
AccessionPrimary (citable) accession number: P0ABB0
Secondary accession number(s): P00822, Q2M852, Q47249
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene