ATP synthase subunit a - Escherichia coli (strain K12)

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P0AB98 (ATP6_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
ATP synthase subunit a

Alternative name(s):
ATP synthase F0 sector subunit a
F-ATPase subunit 6

Gene names

Name:	atpB
Synonyms:	papD, uncB
Ordered Locus Names:	b3738, JW3716

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. HAMAP-Rule MF_01393
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.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.19.
Sequence similarities	Belongs to the ATPase A chain family.
Caution	Was originally (Ref.3) proposed to be encoded from either Met-1 or Val-71 (PID CAA23521); it is now thought to start of Met-1.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	integral to membrane Inferred from direct assay PubMed 2863271. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from mutant phenotype PubMed 6460031. Source: EcoliWiki
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from mutant phenotype PubMed 2863271. Source: EcoCyc proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 2863271. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

ATP synthase subunit a HAMAP-Rule MF_01393

PRO_0000082053

Regions

Topological domain

1 – 39

Periplasmic Probable

Transmembrane

40 – 60

Helical; Probable

Topological domain

61 – 99

Cytoplasmic Probable

Transmembrane

100 – 120

Helical; Probable

Topological domain

121 – 145

Periplasmic Probable

Transmembrane

146 – 166

Helical; Probable

Topological domain

167 – 219

Cytoplasmic Probable

Transmembrane

220 – 240

Helical; Probable

Topological domain

241

Periplasmic Probable

Transmembrane

242 – 262

Helical; Probable

Topological domain

263 – 271

Cytoplasmic Probable

Experimental info

Mutagenesis

206

S → L: Reduced activity.

Mutagenesis

207

L → Y or F: No change in activity.

Mutagenesis

210

R → K, I, V or E: Completely defective.

Mutagenesis

214

N → H: Completely defective.

Mutagenesis

214

N → V: Reduced activity.

Mutagenesis

217

A → H: Reduced activity.

Mutagenesis

217

A → R: Completely defective.

Mutagenesis

245

H → Y: Reduced activity.

Sequence conflict

V → M in CAA23521. Ref.2

Sequence conflict

179 – 182

TLQP → RCST in CAA23590. Ref.4

Sequence conflict

188

F → S in AAA24740. Ref.6

Secondary structure

271

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB98 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4933EAF09401566D
Show »

FASTA

271

30,303

        10         20         30         40         50         60 
MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV VLGLLFLVLF 

        70         80         90        100        110        120 
RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL IAPLALTIFV WVFLMNLMDL 

       130        140        150        160        170        180 
LPIDLLPYIA EHVLGLPALR VVPSADVNVT LSMALGVFIL ILFYSIKMKG IGGFTKELTL 

       190        200        210        220        230        240 
QPFNHWAFIP VNLILEGVSL LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP 

       250        260        270 
WAIFHILIIT LQAFIFMVLT IVYLSMASEE H

« 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 promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase." Gay N.J., Walker J.E. Nucleic Acids Res. 9:3919-3926(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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].
[4]	"Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits." Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M. Biochem. Biophys. Res. Commun. 103:613-620(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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].
[6]	"Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli." Cai B.D., Simoni R.D. J. Biol. Chem. 261:10043-10050(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"Overproduction of subunit a of the F0 component of proton-translocating ATPase inhibits growth of Escherichia coli cells." Kanazawa H., Kiyasu T., Noumi T., Futai M. J. Bacteriol. 158:300-306(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
[11]	"The promoters of the atp operon of Escherichia coli K12." Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G. Mol. Gen. Genet. 193:64-71(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. Strain: K12.
[12]	"Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase." Kumamoto C.A., Simoni R.D. J. Biol. Chem. 261:10037-10042(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-271.
[13]	"Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit." Cain B.D., Simoni R.D. J. Biol. Chem. 264:3292-3300(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[14]	"Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase." Vik S.B., Lee D., Marshall P.A. J. Bacteriol. 173:4544-4548(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[15]	"A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments." Lewis M.L., Chang J.A., Simoni R.D. J. Biol. Chem. 265:10541-10550(1990) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[16]	"The transmembrane topology of the a subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions." Bjorbaek C., Foersom V., Michelsen O. FEBS Lett. 260:31-34(1990) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[17]	"Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a." Yamada H., Moriyama Y., Maeda M., Futai M. FEBS Lett. 390:34-38(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[18]	"Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase." Valiyaveetil F.I., Fillingame R.H. J. Biol. Chem. 273:16241-16247(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[19]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[20]	"Structural changes linked to proton translocation by subunit c of the ATP synthase." Rastogi V.K., Girvin M.E. Nature 402:263-268(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 95-271.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01594 Genomic DNA. Translation: AAA24731.1.
X01631 Genomic DNA. Translation: CAA25776.1.
V00264 Genomic DNA. Translation: CAA23514.1.
V00266 Genomic DNA. Translation: CAA23520.1.
V00266 Genomic DNA. Translation: CAA23521.1.
V00310 Genomic DNA. Translation: CAA23590.1.
M25464 Genomic DNA. Translation: AAA83869.2.
M14019 Genomic DNA. Translation: AAA24740.1.
L10328 Genomic DNA. Translation: AAA62090.1.
U00096 Genomic DNA. Translation: AAC76761.1.
AP009048 Genomic DNA. Translation: BAE77550.1.
X01383 Genomic DNA. Translation: CAA25641.1.
M29174 Genomic DNA. Translation: AAA24423.1.

PIR

LWEC6. C93732.

RefSeq

NP_418194.1. NC_000913.2.
YP_491691.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C17	NMR	-	M	95-271	[»]

ProteinModelPortal

P0AB98.

SMR

P0AB98. Positions 95-265.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47956N.

IntAct

P0AB98. 1 interaction.

MINT

MINT-1300501.

STRING

511145.b3738.

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.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76761; AAC76761; b3738.
BAE77550; BAE77550; BAE77550.

GeneID

12933606.
948252.

KEGG

ecj:Y75_p3430.
eco:b3738.

PATRIC

32122973. VBIEscCol129921_3862.

Organism-specific databases

EchoBASE

EB0097.

EcoGene

EG10099. atpB.

Phylogenomic databases

eggNOG

COG0356.

HOGENOM

HOG000253872.

K02108.

OMA

YIGEHIF.

ProtClustDB

PRK05815.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPB-MONOMER.
ECOL316407:JW3716-MONOMER.
MetaCyc:ATPB-MONOMER.

Gene expression databases

Genevestigator

P0AB98.

Family and domain databases

Gene3D

1.20.120.220. 1 hit.

HAMAP

MF_01393. ATP_synth_a_bact.

InterPro

IPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]

PANTHER

PTHR11410. PTHR11410. 1 hit.

Pfam

PF00119. ATP-synt_A. 1 hit.
[Graphical view]

PRINTS

PR00123. ATPASEA.

SUPFAM

SSF81336. ATPase_F0_A. 1 hit.

TIGRFAMs

TIGR01131. ATP_synt_6_or_A. 1 hit.

PROSITE

PS00449. ATPASE_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075074.

EvolutionaryTrace

P0AB98.

Entry information

Entry name

ATP6_ECOLI

Accession

Primary (citable) accession number: P0AB98
Secondary accession number(s): P00855

Q47708

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 78 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group 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