ATP synthase subunit alpha - Escherichia coli (strain K12)

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P0ABB0 (ATPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from mutant phenotype PubMed 4256722. Source: EcoliWiki plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from mutant phenotype PubMed 153904. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
atpD	P0ABB4	7	EBI-368707,EBI-368783

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 513

513

ATP synthase subunit alpha HAMAP-Rule MF_01346

PRO_0000144325

Regions

Nucleotide binding

169 – 176

ATP Probable

Sites

Site

373

Required for activity

Experimental info

Mutagenesis

175

K → E: Reduced activity and reduced ATP-binding. Ref.12

Mutagenesis

175

K → I: Reduced activity and loss of ATP-binding. Ref.12

Sequence conflict

T → I in AAA83873. Ref.4

Sequence conflict

239 – 244

PYAGCA → RMPVAL in CAA25780. Ref.4

Sequence conflict

239 – 244

PYAGCA → RMPVAL in AAA24735. Ref.4

Sequence conflict

300 – 302

RAA → MLQ in CAA23519. Ref.2

Secondary structure

513

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABB0 [UniParc].

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

FASTA

513

55,222

        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' referencesShow '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 277:1453-1474(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.

PIR

PWECA. G65176.

RefSeq

NP_418190.1. NC_000913.2.
YP_491695.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8S	X-ray	4.40	A/B/C	1-513	[»]
3OAA	X-ray	3.26	A/B/C/I/J/K/Q/R/S/Y/Z/a	1-513	[»]

ProteinModelPortal

P0ABB0.

SMR

P0ABB0. Positions 24-511.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31845N.

IntAct

P0ABB0. 17 interactions.

MINT

MINT-1251537.

STRING

511145.b3734.

Protein family/group databases

TCDB

3.A.2.1.1. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

2D gel databases

SWISS-2DPAGE

P0ABB0.

Proteomic databases

PaxDb

P0ABB0.

PRIDE

P0ABB0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76757; AAC76757; b3734.
BAE77554; BAE77554; BAE77554.

GeneID

12932824.
948242.

KEGG

ecj:Y75_p3434.
eco:b3734.

PATRIC

32122965. VBIEscCol129921_3858.

Organism-specific databases

EchoBASE

EB0096.

EcoGene

EG10098. atpA.

Phylogenomic databases

eggNOG

COG0056.

HOGENOM

HOG000130111.

K02111.

OMA

DSGRHAL.

ProtClustDB

PRK09281.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0ABB0.

Family and domain databases

Gene3D

2.40.30.20. 1 hit.

HAMAP

MF_01346. ATP_synth_alpha_bact.

InterPro

IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005294. ATPase_F1-cplx_asu.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR018538. HAS-barrel.
[Graphical view]

PANTHER

PTHR15184:SF3. PTHR15184:SF3. 1 hit.

Pfam

PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF09378. HAS-barrel. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.

TIGRFAMs

TIGR00962. atpA. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABB0.

Entry information

Entry name

ATPA_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents