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P0AB98 (ATP6_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271ATP synthase subunit a HAMAP-Rule MF_01393
PRO_0000082053

Regions

Topological domain1 – 3939Periplasmic Probable
Transmembrane40 – 6021Helical; Probable
Topological domain61 – 9939Cytoplasmic Probable
Transmembrane100 – 12021Helical; Probable
Topological domain121 – 14525Periplasmic Probable
Transmembrane146 – 16621Helical; Probable
Topological domain167 – 21953Cytoplasmic Probable
Transmembrane220 – 24021Helical; Probable
Topological domain2411Periplasmic Probable
Transmembrane242 – 26221Helical; Probable
Topological domain263 – 2719Cytoplasmic Probable

Experimental info

Mutagenesis2061S → L: Reduced activity.
Mutagenesis2071L → Y or F: No change in activity.
Mutagenesis2101R → K, I, V or E: Completely defective.
Mutagenesis2141N → H: Completely defective.
Mutagenesis2141N → V: Reduced activity.
Mutagenesis2171A → H: Reduced activity.
Mutagenesis2171A → R: Completely defective.
Mutagenesis2451H → Y: Reduced activity.
Sequence conflict711V → M in CAA23521. Ref.2
Sequence conflict179 – 1824TLQP → RCST in CAA23590. Ref.4
Sequence conflict1881F → S in AAA24740. Ref.6

Secondary structure

.......... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB98 [UniParc].

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

FASTA27130,303
        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' 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 277:1453-1462(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.
PIRLWEC6. C93732.
RefSeqNP_418194.1. NC_000913.3.
YP_491691.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C17NMR-M95-271[»]
ProteinModelPortalP0AB98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47956N.
IntActP0AB98. 2 interactions.
MINTMINT-1300501.
STRING511145.b3738.

Chemistry

ChEMBLCHEMBL1075074.

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.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76761; AAC76761; b3738.
BAE77550; BAE77550; BAE77550.
GeneID12933606.
948252.
KEGGecj:Y75_p3430.
eco:b3738.
PATRIC32122973. VBIEscCol129921_3862.

Organism-specific databases

EchoBASEEB0097.
EcoGeneEG10099. atpB.

Phylogenomic databases

eggNOGCOG0356.
HOGENOMHOG000253872.
KOK02108.
OMASFWVLNI.
OrthoDBEOG6K4054.
PhylomeDBP0AB98.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0AB98.

Family and domain databases

Gene3D1.20.120.220. 1 hit.
HAMAPMF_01393. ATP_synth_a_bact.
InterProIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERPTHR11410. PTHR11410. 1 hit.
PfamPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSPR00123. ATPASEA.
SUPFAMSSF81336. SSF81336. 1 hit.
TIGRFAMsTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEPS00449. ATPASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AB98.
PROP0AB98.

Entry information

Entry nameATP6_ECOLI
AccessionPrimary (citable) accession number: P0AB98
Secondary accession number(s): P00855 expand/collapse secondary AC list , Q2M856, Q47065, Q47708
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 89 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