ATP synthase subunit delta - Escherichia coli (strain K12)

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P0ABA4 (ATPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. 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 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
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	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from mutant phenotype PubMed 6294057. Source: EcoliWiki
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from mutant phenotype PubMed 6294057. Source: EcoCyc proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 6294057. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

ATP synthase subunit delta HAMAP-Rule MF_01416

PRO_0000193462

Experimental info

Sequence conflict

E → D in AAA20044. Ref.4

Secondary structure

177

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABA4 [UniParc].

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

177

19,332

        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' 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 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 277:1453-1474(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.

PIR

PWECD. A93732.

RefSeq

NP_418191.1. NC_000913.2.
YP_491694.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ABV	NMR	-	A	2-135	[»]
2A7U	NMR	-	B	2-135	[»]

ProteinModelPortal

P0ABA4.

SMR

P0ABA4. Positions 2-135.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47921N.

IntAct

P0ABA4. 7 interactions.

STRING

511145.b3735.

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.

Proteomic databases

PaxDb

P0ABA4.

PRIDE

P0ABA4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76758; AAC76758; b3735.
BAE77553; BAE77553; BAE77553.

GeneID

12933117.
948254.

KEGG

ecj:Y75_p3433.
eco:b3735.

PATRIC

32122967. VBIEscCol129921_3859.

Organism-specific databases

EchoBASE

EB0103.

EcoGene

EG10105. atpH.

Phylogenomic databases

eggNOG

COG0712.

HOGENOM

HOG000075824.

K02113.

OMA

CGEQINE.

ProtClustDB

PRK05758.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0ABA4.

Family and domain databases

Gene3D

1.10.520.20. 1 hit.

HAMAP

MF_01416. ATP_synth_delta_bact.

InterPro

IPR000711. ATPase_F1-cplx_OSCP/dsu.
IPR020781. ATPase_F1-cplx_OSCP/dsu_CS.
IPR026015. ATPase_OSCP/delta_N.
[Graphical view]

PANTHER

PTHR11910. PTHR11910. 1 hit.

Pfam

PF00213. OSCP. 1 hit.
[Graphical view]

PRINTS

PR00125. ATPASEDELTA.

SUPFAM

SSF47928. ATPsynt_OSCP. 1 hit.

TIGRFAMs

TIGR01145. ATP_synt_delta. 1 hit.

PROSITE

PS00389. ATPASE_DELTA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABA4.

Entry information

Entry name

ATPD_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 73 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

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic 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