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Protein

ATP synthase subunit a

Gene

atpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.

GO - Molecular functioni

  1. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  1. plasma membrane ATP synthesis coupled proton transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:ATPB-MONOMER.
ECOL316407:JW3716-MONOMER.
MetaCyc:ATPB-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 aUniRule annotation
Alternative name(s):
ATP synthase F0 sector subunit aUniRule annotation
F-ATPase subunit 6UniRule annotation
Gene namesi
Name:atpBUniRule annotation
Synonyms:papD, uncB
Ordered Locus Names:b3738, JW3716
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10099. atpB.

Subcellular locationi

Cell inner membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3939PeriplasmicCuratedAdd
BLAST
Transmembranei40 – 6021HelicalCuratedAdd
BLAST
Topological domaini61 – 9939CytoplasmicCuratedAdd
BLAST
Transmembranei100 – 12021HelicalCuratedAdd
BLAST
Topological domaini121 – 14525PeriplasmicCuratedAdd
BLAST
Transmembranei146 – 16621HelicalCuratedAdd
BLAST
Topological domaini167 – 21953CytoplasmicCuratedAdd
BLAST
Transmembranei220 – 24021HelicalCuratedAdd
BLAST
Topological domaini241 – 2411PeriplasmicCurated
Transmembranei242 – 26221HelicalCuratedAdd
BLAST
Topological domaini263 – 2719CytoplasmicCurated

GO - Cellular componenti

  1. integral component of membrane Source: EcoliWiki
  2. integral component of plasma membrane Source: EcoCyc
  3. proton-transporting ATP synthase complex, coupling factor F(o) Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(0), Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061S → L: Reduced activity.
Mutagenesisi207 – 2071L → Y or F: No change in activity.
Mutagenesisi210 – 2101R → K, I, V or E: Completely defective.
Mutagenesisi214 – 2141N → H: Completely defective.
Mutagenesisi214 – 2141N → V: Reduced activity.
Mutagenesisi217 – 2171A → H: Reduced activity.
Mutagenesisi217 – 2171A → R: Completely defective.
Mutagenesisi245 – 2451H → Y: Reduced activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271ATP synthase subunit aPRO_0000082053Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0AB98.

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.

Protein-protein interaction databases

DIPiDIP-47956N.
IntActiP0AB98. 2 interactions.
MINTiMINT-1300501.
STRINGi511145.b3738.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi97 – 12529Combined sources
Helixi135 – 16632Combined sources
Helixi202 – 22827Combined sources
Beta strandi229 – 2313Combined sources
Helixi233 – 26331Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C17NMR-M95-271[»]
ProteinModelPortaliP0AB98.
SMRiP0AB98. Positions 95-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB98.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0356.
HOGENOMiHOG000253872.
InParanoidiP0AB98.
KOiK02108.
OMAiHLQNIKQ.
OrthoDBiEOG6K4054.
PhylomeDBiP0AB98.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AB98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV
60 70 80 90 100
VLGLLFLVLF RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL
110 120 130 140 150
IAPLALTIFV WVFLMNLMDL LPIDLLPYIA EHVLGLPALR VVPSADVNVT
160 170 180 190 200
LSMALGVFIL ILFYSIKMKG IGGFTKELTL QPFNHWAFIP VNLILEGVSL
210 220 230 240 250
LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP WAIFHILIIT
260 270
LQAFIFMVLT IVYLSMASEE H
Length:271
Mass (Da):30,303
Last modified:July 21, 1986 - v1
Checksum:i4933EAF09401566D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711V → M in CAA23521 (PubMed:6272190).Curated
Sequence conflicti179 – 1824TLQP → RCST in CAA23590 (PubMed:6277311).Curated
Sequence conflicti188 – 1881F → S in AAA24740 (PubMed:2874137).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC93732. LWEC6.
RefSeqiNP_418194.1. NC_000913.3.
YP_491691.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76761; AAC76761; b3738.
BAE77550; BAE77550; BAE77550.
GeneIDi12933606.
948252.
KEGGiecj:Y75_p3430.
eco:b3738.
PATRICi32122973. VBIEscCol129921_3862.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC93732. LWEC6.
RefSeqiNP_418194.1. NC_000913.3.
YP_491691.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C17NMR-M95-271[»]
ProteinModelPortaliP0AB98.
SMRiP0AB98. Positions 95-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47956N.
IntActiP0AB98. 2 interactions.
MINTiMINT-1300501.
STRINGi511145.b3738.

Chemistry

ChEMBLiCHEMBL1075074.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76761; AAC76761; b3738.
BAE77550; BAE77550; BAE77550.
GeneIDi12933606.
948252.
KEGGiecj:Y75_p3430.
eco:b3738.
PATRICi32122973. VBIEscCol129921_3862.

Organism-specific databases

EchoBASEiEB0097.
EcoGeneiEG10099. atpB.

Phylogenomic databases

eggNOGiCOG0356.
HOGENOMiHOG000253872.
InParanoidiP0AB98.
KOiK02108.
OMAiHLQNIKQ.
OrthoDBiEOG6K4054.
PhylomeDBiP0AB98.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AB98.
PROiP0AB98.

Gene expression databases

GenevestigatoriP0AB98.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiATP6_ECOLI
AccessioniPrimary (citable) accession number: P0AB98
Secondary accession number(s): P00855
, Q2M856, Q47065, Q47708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally proposed to be encoded from either Met-1 or Val-71 (PID CAA23521); it is now thought to start of Met-1.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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 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.