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Protein

ATP synthase subunit delta

Gene

atpH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.
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.

GO - Molecular functioni

  • proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
  • proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:ATPH-MONOMER.
MetaCyc:ATPH-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 deltaUniRule annotation
Alternative name(s):
ATP synthase F(1) sector subunit deltaUniRule annotation
F-type ATPase subunit deltaUniRule annotation
Short name:
F-ATPase subunit deltaUniRule annotation
Gene namesi
Name:atpHUniRule annotation
Synonyms:papE, uncH
Ordered Locus Names:b3735, JW3713
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10105. atpH.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: UniProtKB-SubCell
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001934621 – 177ATP synthase subunit deltaAdd BLAST177

Proteomic databases

PaxDbiP0ABA4.
PRIDEiP0ABA4.

Interactioni

Subunit structurei

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.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-47921N.
IntActiP0ABA4. 13 interactors.
STRINGi316385.ECDH10B_3922.

Structurei

Secondary structure

1177
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 21Combined sources17
Helixi25 – 39Combined sources15
Helixi42 – 48Combined sources7
Helixi54 – 65Combined sources12
Helixi71 – 82Combined sources12
Helixi86 – 88Combined sources3
Helixi89 – 105Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABVNMR-A2-135[»]
2A7UNMR-B2-135[»]
5T4Oelectron microscopy6.90L1-177[»]
5T4Pelectron microscopy7.77L1-177[»]
5T4Qelectron microscopy8.53L1-177[»]
ProteinModelPortaliP0ABA4.
SMRiP0ABA4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABA4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase delta chain family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107S15. Bacteria.
COG0712. LUCA.
HOGENOMiHOG000075824.
InParanoidiP0ABA4.
KOiK02113.
PhylomeDBiP0ABA4.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact. 1 hit.
InterProiView protein in InterPro
IPR026015. ATP_synth_OSCP/delta_N.
IPR020781. ATPase_OSCP/d_CS.
IPR000711. ATPase_OSCP/dsu.
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiView protein in Pfam
PF00213. OSCP. 1 hit.
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
PROSITEiView protein in PROSITE
PS00389. ATPASE_DELTA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ABA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG
60 70 80 90 100
ALAPETLAES FIAVCGEQLD ENGQNLIRVM AENGRLNALP DVLEQFIHLR
110 120 130 140 150
AVSEATAEVD VISAAALSEQ QLAKISAAME KRLSRKVKLN CKIDKSVMAG
160 170
VIIRAGDMVI DGSVRGRLER LADVLQS
Length:177
Mass (Da):19,332
Last modified:July 21, 1986 - v1
Checksum:i6AFD9552A79C81A5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82E → D in AAA20044 (PubMed:6458296).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA93732. PWECD.
RefSeqiNP_418191.1. NC_000913.3.
WP_001288587.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76758; AAC76758; b3735.
BAE77553; BAE77553; BAE77553.
GeneIDi948254.
KEGGiecj:JW3713.
eco:b3735.
PATRICifig|1411691.4.peg.2965.

Similar proteinsi

Entry informationi

Entry nameiATPD_ECOLI
AccessioniPrimary (citable) accession number: P0ABA4
Secondary accession number(s): P00831, Q2M853
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 30, 2017
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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