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P0ABA4 (ATPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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 delta
Alternative name(s):
ATP synthase F(1) sector subunit delta
F-type ATPase subunit delta
Short name=F-ATPase subunit delta
Gene names
Name:atpH
Synonyms:papE, uncH
Ordered Locus Names:b3735, JW3713
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. HAMAP-Rule MF_01416

This protein is part of the stalk that links CF0 to CF1. It either transmits conformational changes from CF0 to CF1 or is implicated in proton conduction. HAMAP-Rule MF_01416

Subunit structure

F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Ref.9

Subcellular location

Cell inner membrane; Peripheral membrane protein Ref.9.

Sequence similarities

Belongs to the ATPase delta chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177ATP synthase subunit delta HAMAP-Rule MF_01416
PRO_0000193462

Experimental info

Sequence conflict821E → D in AAA20044. Ref.4

Secondary structure

.............. 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABA4 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 6AFD9552A79C81A5

FASTA17719,332
        10         20         30         40         50         60 
MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG ALAPETLAES 

        70         80         90        100        110        120 
FIAVCGEQLD ENGQNLIRVM AENGRLNALP DVLEQFIHLR AVSEATAEVD VISAAALSEQ 

       130        140        150        160        170 
QLAKISAAME KRLSRKVKLN CKIDKSVMAG VIIRAGDMVI DGSVRGRLER LADVLQS 

« 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 gene coding for the delta subunit of proton translocating ATPase of Escherichia coli."
Mabuchi K., Kanazawa H., Kayano T., Futai M.
Biochem. Biophys. Res. Commun. 102:172-179(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]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase."
Wilkens S., Dunn S.D., Chandler J., Dahlquist F.W., Capaldi R.A.
Nat. Struct. Biol. 4:198-201(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-135.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01594 Genomic DNA. Translation: AAA24734.1.
M12212 Unassigned DNA. Translation: AAA20044.1.
X01631 Genomic DNA. Translation: CAA25779.1.
V00266 Genomic DNA. Translation: CAA23524.1.
V00264 Genomic DNA. Translation: CAA23517.1.
M25464 Genomic DNA. Translation: AAA83872.1.
L10328 Genomic DNA. Translation: AAA62087.1.
U00096 Genomic DNA. Translation: AAC76758.1.
AP009048 Genomic DNA. Translation: BAE77553.1.
PIRPWECD. A93732.
RefSeqNP_418191.1. NC_000913.3.
YP_491694.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ABVNMR-A2-135[»]
2A7UNMR-B2-135[»]
ProteinModelPortalP0ABA4.
SMRP0ABA4. Positions 2-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47921N.
IntActP0ABA4. 13 interactions.
STRING511145.b3735.

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.

Proteomic databases

PaxDbP0ABA4.
PRIDEP0ABA4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76758; AAC76758; b3735.
BAE77553; BAE77553; BAE77553.
GeneID12933117.
948254.
KEGGecj:Y75_p3433.
eco:b3735.
PATRIC32122967. VBIEscCol129921_3859.

Organism-specific databases

EchoBASEEB0103.
EcoGeneEG10105. atpH.

Phylogenomic databases

eggNOGCOG0712.
HOGENOMHOG000075824.
KOK02113.
OMACGEQINE.
OrthoDBEOG6DNTDK.
PhylomeDBP0ABA4.
ProtClustDBPRK05758.

Enzyme and pathway databases

BioCycEcoCyc:ATPH-MONOMER.
ECOL316407:JW3713-MONOMER.
MetaCyc:ATPH-MONOMER.

Gene expression databases

GenevestigatorP0ABA4.

Family and domain databases

Gene3D1.10.520.20. 1 hit.
HAMAPMF_01416. ATP_synth_delta_bact.
InterProIPR000711. ATPase_F1-cplx_OSCP/dsu.
IPR020781. ATPase_F1-cplx_OSCP/dsu_CS.
IPR026015. ATPase_OSCP/delta_N.
[Graphical view]
PANTHERPTHR11910. PTHR11910. 1 hit.
PfamPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSPR00125. ATPASEDELTA.
SUPFAMSSF47928. SSF47928. 1 hit.
TIGRFAMsTIGR01145. ATP_synt_delta. 1 hit.
PROSITEPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABA4.
PROP0ABA4.

Entry information

Entry nameATPD_ECOLI
AccessionPrimary (citable) accession number: P0ABA4
Secondary accession number(s): P00831, Q2M853
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 80 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