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A5VNW5 (ATPF2_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP synthase subunit b 2
Alternative name(s):
ATP synthase F(0) sector subunit b 2
ATPase subunit I 2
F-type ATPase subunit b 2
Short name=F-ATPase subunit b 2
Gene names
Name:atpF2
Ordered Locus Names:BOV_0397
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length159 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 MF_01398

Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP MF_01398

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; Single-pass membrane protein By similarity HAMAP MF_01398.

Sequence similarities

Belongs to the ATPase B chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 159159ATP synthase subunit b 2 HAMAP MF_01398
PRO_0000368373

Regions

Transmembrane1 – 2121Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A5VNW5 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 68FF2AE85B4E8211

FASTA15917,441
        10         20         30         40         50         60 
MDATFWAFIA LVIFVAIVVY MKVPGMIGRT LDERADRIKK ELEEARTLRE EAQQLLAEYH 

        70         80         90        100        110        120 
RKCKEAEKEA GDIVASAERE AKALLEEAKR ATEEYVARRN KLAEQKIATA ETDAINAVRA 

       130        140        150 
SAVDLAVAAA GSILAEKVDA KAAGNLFNDA LAQVKSHLN 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000708 Genomic DNA. Translation: ABQ60781.1.
RefSeqYP_001258412.1. NC_009505.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5VNW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5201921.
GenomeReviewsGene locus BOV_0397 in contig CP000708_GR.
KEGGbov:BOV_0397.
PATRIC17860580. VBIBruOvi136990_1708.
TIGRBOV_0397.

Phylogenomic databases

HOGENOMHBG692690.
OMAAKMEDFV.
ProtClustDBPRK09173.

Family and domain databases

HAMAPMF_01398. ATP_synth_b_bact.
[Tree]
InterProIPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
KOK02109.
PfamPF00430. ATP-synt_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR01144. ATP_synt_b. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATPF2_BRUO2
AccessionPrimary (citable) accession number: A5VNW5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 36 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