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B2VCA8 (ATPF_ERWT9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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
Alternative name(s):
ATP synthase F(0) sector subunit b
ATPase subunit I
F-type ATPase subunit b
Short name=F-ATPase subunit b
Gene names
Name:atpF
Ordered Locus Names:ETA_34790
OrganismErwinia tasmaniensis (strain DSM 17950 / Et1/99) [Complete proteome] [HAMAP]
Taxonomic identifier338565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia

Protein attributes

Sequence length156 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 – 156156ATP synthase subunit b HAMAP MF_01398
PRO_0000368471

Regions

Transmembrane11 – 3121Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
B2VCA8 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: A0521017E6166F78

FASTA15617,260
        10         20         30         40         50         60 
MNINATILGQ AIAFILFVAF CMKYVWPPLM AAIEKRQKEV ADGLASAERA KKDLDLAQAS 

        70         80         90        100        110        120 
ATDQLKKAKD DAQVIIEQAN KRRAQILDDA KAEAEQERNK IVTQAQAEID AERKRAREEL 

       130        140        150 
RKQVAMLAVA GAEKIIERSV DEAANSDIVD KLVAEL 

« Hide

References

[1]"The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic bacterium in the genus Erwinia."
Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., Geider K.
Environ. Microbiol. 10:2211-2222(2008) [PubMed: 18462403] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17950 / Et1/99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468135 Genomic DNA. Translation: CAO98525.1.
RefSeqYP_001909384.1. NC_010694.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6297841.
GenomeReviewsGene locus ETA_34790 in contig CU468135_GR.
PATRIC20432889. VBIErwTas9546_3571.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG617328.
OMALEKYNAQ.
ProtClustDBPRK05759.

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]
PfamPF00430. ATP-synt_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR01144. ATP_synt_b. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATPF_ERWT9
AccessionPrimary (citable) accession number: B2VCA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 25 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