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A9IQI8 (ATPF2_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:BT_0625
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length164 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 – 164164ATP synthase subunit b 2 HAMAP MF_01398
PRO_0000368347

Regions

Transmembrane4 – 2421Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A9IQI8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 138B4BCE94EFB79C

FASTA16418,566
        10         20         30         40         50         60 
MSDTFWAFVG LVLFLALLVY FQIPQKIIHH LDARAKRIKD ELDEALRLRE EAQEILAEYQ 

        70         80         90        100        110        120 
RKHAEAEKDA QEIIAAAKHE VESVIAEART KAEEYVKNRN KLAEQKIAQA EADAIRMVSS 

       130        140        150        160 
SAIDLAISTA RVLIAKELDS NRADELVKEA LSKESLSKMK THLN 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK01063.1.
RefSeqYP_001609058.1. NC_010161.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA9IQI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829825.
GenomeReviewsGene locus BT_0625 in contig AM260525_GR.
PATRIC20549006. VBIBarTri113218_0662.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG692690.
OMAAKMEDFV.
ProtClustDBPRK09173.

Enzyme and pathway databases

BioCycBTRI382640:BT_0625-MONOMER.

Family and domain databases

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

Entry information

Entry nameATPF2_BART1
AccessionPrimary (citable) accession number: A9IQI8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 29 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