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P0ABB0

- ATPA_ECOLI

UniProt

P0ABB0 - ATPA_ECOLI

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Protein

ATP synthase subunit alpha

Gene

atpA

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

Functioni

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

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei373 – 3731Required for activity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1768ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB-HAMAP

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: EcoliWiki
  3. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPA-MONOMER.
ECOL316407:JW3712-MONOMER.
MetaCyc:ATPA-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 alphaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit alphaUniRule annotation
F-ATPase subunit alphaUniRule annotation
Gene namesi
Name:atpAUniRule annotation
Synonyms:papA, uncA
Ordered Locus Names:b3734, JW3712
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10098. atpA.

Subcellular locationi

Cell inner membrane 1 PublicationUniRule annotation; Peripheral membrane protein 1 PublicationUniRule annotation

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB-HAMAP
  3. proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi175 – 1751K → E: Reduced activity and reduced ATP-binding. 1 Publication
Mutagenesisi175 – 1751K → I: Reduced activity and loss of ATP-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513ATP synthase subunit alphaPRO_0000144325Add
BLAST

Proteomic databases

PaxDbiP0ABB0.
PRIDEiP0ABB0.

2D gel databases

SWISS-2DPAGEP0ABB0.

Expressioni

Gene expression databases

GenevestigatoriP0ABB0.

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.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
atpDP0ABB410EBI-368707,EBI-368783

Protein-protein interaction databases

DIPiDIP-31845N.
IntActiP0ABB0. 28 interactions.
MINTiMINT-1251537.
STRINGi511145.b3734.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358Combined sources
Beta strandi38 – 436Combined sources
Beta strandi52 – 554Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 668Combined sources
Beta strandi71 – 777Combined sources
Beta strandi87 – 893Combined sources
Beta strandi94 – 985Combined sources
Helixi101 – 1033Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi136 – 1383Combined sources
Helixi151 – 1566Combined sources
Beta strandi166 – 1749Combined sources
Helixi175 – 18410Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi192 – 1998Combined sources
Helixi202 – 21514Combined sources
Beta strandi221 – 2266Combined sources
Helixi232 – 25120Combined sources
Beta strandi255 – 2617Combined sources
Helixi263 – 27614Combined sources
Helixi290 – 2989Combined sources
Beta strandi302 – 3043Combined sources
Helixi306 – 3138Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 3353Combined sources
Helixi340 – 3489Combined sources
Beta strandi349 – 3557Combined sources
Helixi357 – 3604Combined sources
Turni370 – 3723Combined sources
Beta strandi374 – 3774Combined sources
Helixi378 – 3814Combined sources
Helixi384 – 40724Combined sources
Helixi415 – 43016Combined sources
Helixi443 – 45210Combined sources
Turni455 – 4595Combined sources
Helixi462 – 47514Combined sources
Helixi477 – 4793Combined sources
Helixi481 – 4899Combined sources
Helixi494 – 50714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40A/B/C1-513[»]
3OAAX-ray3.26A/B/C/I/J/K/Q/R/S/Y/Z/a1-513[»]
ProteinModelPortaliP0ABB0.
SMRiP0ABB0. Positions 24-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABB0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0056.
HOGENOMiHOG000130111.
InParanoidiP0ABB0.
KOiK02111.
OMAiNDEIKDT.
OrthoDBiEOG67X1S1.
PhylomeDBiP0ABB0.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. 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]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF09378. HAS-barrel. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABB0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG
60 70 80 90 100
EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG
110 120 130 140 150
RGLLGRVVNT LGAPIDGKGP LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY
160 170 180 190 200
KAVDSMIPIG RGQRELIIGD RQTGKTALAI DAIINQRDSG IKCIYVAIGQ
210 220 230 240 250
KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY AGCAMGEYFR
260 270 280 290 300
DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
310 320 330 340 350
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD
360 370 380 390 400
GQIFLETNLF NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY
410 420 430 440 450
RELAAFSQFA SDLDDATRKQ LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA
460 470 480 490 500
AERGYLADVE LSKIGSFEAA LLAYVDRDHA PLMQEINQTG GYNDEIEGKL
510
KGILDSFKAT QSW
Length:513
Mass (Da):55,222
Last modified:November 8, 2005 - v1
Checksum:iDD1F3859375E9103
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911T → I in AAA83873. (PubMed:6301339)Curated
Sequence conflicti239 – 2446PYAGCA → RMPVAL in CAA25780. (PubMed:6301339)Curated
Sequence conflicti239 – 2446PYAGCA → RMPVAL in AAA24735. (PubMed:6301339)Curated
Sequence conflicti300 – 3023RAA → MLQ in CAA23519. (PubMed:6272228)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG65176. PWECA.
RefSeqiNP_418190.1. NC_000913.3.
YP_491695.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76757; AAC76757; b3734.
BAE77554; BAE77554; BAE77554.
GeneIDi12932824.
948242.
KEGGiecj:Y75_p3434.
eco:b3734.
PATRICi32122965. VBIEscCol129921_3858.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi G65176. PWECA.
RefSeqi NP_418190.1. NC_000913.3.
YP_491695.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P0ABB0.
SMRi P0ABB0. Positions 24-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31845N.
IntActi P0ABB0. 28 interactions.
MINTi MINT-1251537.
STRINGi 511145.b3734.

Protein family/group databases

TCDBi 3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGE P0ABB0.

Proteomic databases

PaxDbi P0ABB0.
PRIDEi P0ABB0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76757 ; AAC76757 ; b3734 .
BAE77554 ; BAE77554 ; BAE77554 .
GeneIDi 12932824.
948242.
KEGGi ecj:Y75_p3434.
eco:b3734.
PATRICi 32122965. VBIEscCol129921_3858.

Organism-specific databases

EchoBASEi EB0096.
EcoGenei EG10098. atpA.

Phylogenomic databases

eggNOGi COG0056.
HOGENOMi HOG000130111.
InParanoidi P0ABB0.
KOi K02111.
OMAi NDEIKDT.
OrthoDBi EOG67X1S1.
PhylomeDBi P0ABB0.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P0ABB0.
PROi P0ABB0.

Gene expression databases

Genevestigatori P0ABB0.

Family and domain databases

Gene3Di 2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01346. ATP_synth_alpha_bact.
InterProi IPR020003. 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 ]
PANTHERi PTHR15184:SF3. PTHR15184:SF3. 1 hit.
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF09378. HAS-barrel. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00962. atpA. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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. 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. 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. 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.

Entry informationi

Entry nameiATPA_ECOLI
AccessioniPrimary (citable) accession number: P0ABB0
Secondary accession number(s): P00822, Q2M852, Q47249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 8, 2005
Last modified: November 26, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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