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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Acinetobacter baumannii (strain ACICU)
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi148 – 155ATPUniRule annotation8

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

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:ACICU_00178
OrganismiAcinetobacter baumannii (strain ACICU)
Taxonomic identifieri405416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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)DescriptionActionsGraphical viewLength
ChainiPRO_10001434621 – 464ATP synthase subunit betaAdd BLAST464

Proteomic databases

PRIDEiB2I102.

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

Structurei

3D structure databases

ProteinModelPortaliB2I102.
SMRiB2I102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2I102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGRIIQII GAVIDVEFER TSVPKIYDAL QVDGTETTLE VQQQLGDGVV
60 70 80 90 100
RTIAMGSTEG LKRGLTVTST NAPISVPVGT ATLGRIMDVL GRPIDEAGPV
110 120 130 140 150
ATEERLPIHR QAPSYAEQAA STDLLETGIK VIDLLCPFAK GGKVGLFGGA
160 170 180 190 200
GVGKTVNMME LINNIAKAHS GLSVFAGVGE RTREGNDFYH EMKDSNVLDK
210 220 230 240 250
VAMVYGQMNE PPGNRLRVAL TGLTMAEYFR DEKDENGKGR DVLLFVDNIY
260 270 280 290 300
RYTLAGTEVS ALLGRMPSAV GYQPTLAEEM GVLQERITST KSGSITSIQA
310 320 330 340 350
VYVPADDLTD PSPATTFAHL DATVVLSRDI ASSGIYPAID PLDSTSRQLD
360 370 380 390 400
PLVVGQEHYE IARAVQNVLQ RYKELKDIIA ILGMDELAEE DKLVVYRARK
410 420 430 440 450
IQRFFSQPFH VAEVFTGAPG KLVPLKETIR GFKGLLAGEY DHIPEQAFYM
460
VGGIDEVIAK AEKL
Length:464
Mass (Da):50,274
Last modified:June 10, 2008 - v1
Checksum:i6D679361227BC1D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000863 Genomic DNA. Translation: ACC55490.1.
RefSeqiWP_000094481.1. NC_010611.1.

Genome annotation databases

EnsemblBacteriaiACC55490; ACC55490; ACICU_00178.
KEGGiabc:ACICU_00178.
PATRICi20709106. VBIAciBau103538_0278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000863 Genomic DNA. Translation: ACC55490.1.
RefSeqiWP_000094481.1. NC_010611.1.

3D structure databases

ProteinModelPortaliB2I102.
SMRiB2I102.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB2I102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC55490; ACC55490; ACICU_00178.
KEGGiabc:ACICU_00178.
PATRICi20709106. VBIAciBau103538_0278.

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATPB_ACIBC
AccessioniPrimary (citable) accession number: B2I102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.