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Protein

ATP synthase subunit delta

Gene

atpH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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

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

EPDiP0ABA4
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

BioGridi4262111, 51 interactors
DIPiDIP-47921N
IntActiP0ABA4, 13 interactors
STRINGi316385.ECDH10B_3922

Structurei

Secondary structure

1177
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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_sf
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

Cross-referencesi

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

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...

Protein-protein interaction databases

BioGridi4262111, 51 interactors
DIPiDIP-47921N
IntActiP0ABA4, 13 interactors
STRINGi316385.ECDH10B_3922

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

Proteomic databases

EPDiP0ABA4
PaxDbiP0ABA4
PRIDEiP0ABA4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0103
EcoGeneiEG10105 atpH

Phylogenomic databases

eggNOGiENOG4107S15 Bacteria
COG0712 LUCA
HOGENOMiHOG000075824
InParanoidiP0ABA4
KOiK02113
PhylomeDBiP0ABA4

Enzyme and pathway databases

BioCyciEcoCyc:ATPH-MONOMER
MetaCyc:ATPH-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ABA4
PROiPR:P0ABA4

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_sf
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
ProtoNetiSearch...

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: November 7, 2018
This is version 108 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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