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A5VNW4 (ATPF1_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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 1
Alternative name(s):
ATP synthase F(0) sector subunit b 1
ATPase subunit I 1
F-type ATPase subunit b 1
Short name=F-ATPase subunit b 1
Gene names
Name:atpF1
Ordered Locus Names:BOV_0396
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length208 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 – 208208ATP synthase subunit b 1 HAMAP MF_01398
PRO_0000368372

Regions

Transmembrane56 – 7823Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A5VNW4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 0EE57A31D20BC6E8

FASTA20821,896
        10         20         30         40         50         60 
MFVSTAFAQT ATESQPASTA GEHGAADAVH TETGVAHDAG HGSGVFPPFD STHYASQVLW 

        70         80         90        100        110        120 
LAITFGLFYL FLSRVVLPRI GGVIETRRDR IAQDLEQAAR LKQDADNAIA AYEQELAQAR 

       130        140        150        160        170        180 
SKAASIAEAA REKGKGEADA ERASAEAVLE SKLKEAEERI AAIKAKAMSD VGNIAEETTA 

       190        200 
TIVEQLLGLT ADKASVSEAV KAIRASNA 

« 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: ABQ61216.1.
RefSeqYP_001258411.1. NC_009505.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5VNW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5203395.
GenomeReviewsGene locus BOV_0396 in contig CP000708_GR.
KEGGbov:BOV_0396.
PATRIC17860578. VBIBruOvi136990_1707.
TIGRBOV_0396.

Phylogenomic databases

HOGENOMHBG656755.
OMALEKYNAQ.
ProtClustDBPRK09174.

Family and domain databases

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

Entry information

Entry nameATPF1_BRUO2
AccessionPrimary (citable) accession number: A5VNW4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 35 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