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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1688ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciADEH290397:GI2Z-4406-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit betaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit betaUniRule annotation
F-ATPase subunit betaUniRule annotation
Gene namesi
Name:atpDUniRule annotation
Ordered Locus Names:Adeh_4348
OrganismiAnaeromyxobacter dehalogenans (strain 2CP-C)
Taxonomic identifieri290397 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
Proteomesi
  • UP000001935 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482ATP synthase subunit betaPRO_0000254201Add
BLAST

Proteomic databases

PRIDEiQ2IHQ2.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

Protein-protein interaction databases

STRINGi290397.Adeh_4348.

Structurei

3D structure databases

ProteinModelPortaliQ2IHQ2.
SMRiQ2IHQ2. Positions 10-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
KOiK02112.
OMAiAEFGIYP.
OrthoDBiEOG6HQSP3.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2IHQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTATNVENG RITQVIGPVV DVEFPPGTLP DIYTALKVTN PGVDERQDNL
60 70 80 90 100
VIEVAQHLGE NTARCIAMDS TEGLVRGMPV KNTGAPISVP VGQEVLGRIL
110 120 130 140 150
NVVGEPVDER GPVAATKTLP IHRSAPLLTD LNVKVESFET GIKVIDLLAP
160 170 180 190 200
YLRGGKIGLF GGAGVGKTVL LMELVNNVAK KRGGFSVFGG VGERTREGND
210 220 230 240 250
LYHEMIEAGV INKDDLSKSQ CVLVYGQMNE PPGARARVAL SALTVAEYFR
260 270 280 290 300
DVENRDMLLF IDNIFRFTQA GSEVSALLGR IPSAVGYQPT LSTEMGELQE
310 320 330 340 350
RITSTQKGAI TSVQAIYVPA DDLTDPAPAT AFAHLDATTV LNRKLTEIGI
360 370 380 390 400
YPAVDPLDST SRILDPNVVG KEHYAVARAV QETLQRYKDL QDIIAILGMD
410 420 430 440 450
ELSEDDKLTV ARARKIQRFL SQPFTVAQQF TGNPGKYVEL PDTIRGFKEI
460 470 480
VDGKHDDLPE QAFYMVGGIE EAVEKAKKLT AG
Length:482
Mass (Da):52,132
Last modified:March 7, 2006 - v1
Checksum:i4361AC18EF4E4089
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000251 Genomic DNA. Translation: ABC84111.1.
RefSeqiWP_011423393.1. NC_007760.1.

Genome annotation databases

EnsemblBacteriaiABC84111; ABC84111; Adeh_4348.
KEGGiade:Adeh_4348.
PATRICi20924996. VBIAnaDeh31384_4451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000251 Genomic DNA. Translation: ABC84111.1.
RefSeqiWP_011423393.1. NC_007760.1.

3D structure databases

ProteinModelPortaliQ2IHQ2.
SMRiQ2IHQ2. Positions 10-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290397.Adeh_4348.

Proteomic databases

PRIDEiQ2IHQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC84111; ABC84111; Adeh_4348.
KEGGiade:Adeh_4348.
PATRICi20924996. VBIAnaDeh31384_4451.

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
KOiK02112.
OMAiAEFGIYP.
OrthoDBiEOG6HQSP3.

Enzyme and pathway databases

BioCyciADEH290397:GI2Z-4406-MONOMER.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2CP-C.

Entry informationi

Entry nameiATPB_ANADE
AccessioniPrimary (citable) accession number: Q2IHQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 7, 2006
Last modified: May 11, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.