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Q83AF8 (ATPD_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:CBU_1942
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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 By similarity. 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 By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_01416.

Sequence similarities

Belongs to the ATPase delta chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185ATP synthase subunit delta HAMAP-Rule MF_01416
PRO_1000184686

Sequences

Sequence LengthMass (Da)Tools
Q83AF8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E421BF892526E3FB

FASTA18521,189
        10         20         30         40         50         60 
MALHLTLARP YAKAAFADGQ KANQLEAWLA VFTAFSKIIK NKEVARQIIN PKFSDKEIKT 

        70         80         90        100        110        120 
LLFDLIQTIE PESTKQLKDK IDHFLQLLID EKRLMILPDI ALVYQQLLNK YQGIIEASVT 

       130        140        150        160        170        180 
YVFPLNDEHR QQIQKQLEKR FNAEVKLKMI KDESLLGGVI IRAGNWVMDG SIKGKLTRLA 


ENLKG 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO91432.1.
RefSeqNP_820918.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83AF8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO91432; AAO91432; CBU_1942.
GeneID1209855.
KEGGcbu:CBU_1942.
PATRIC17932623. VBICoxBur82552_1928.

Phylogenomic databases

eggNOGCOG0712.
HOGENOMHOG000075824.
KOK02113.
OMACGEQINE.
OrthoDBEOG6DNTDK.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1916-MONOMER.

Family and domain databases

Gene3D1.10.520.20. 1 hit.
HAMAPMF_01416. ATP_synth_delta_bact.
InterProIPR000711. ATPase_F1-cplx_OSCP/dsu.
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.
ProtoNetSearch...

Entry information

Entry nameATPD_COXBU
AccessionPrimary (citable) accession number: Q83AF8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 65 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names