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Q0BJL9 (ATPF_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Bamb_0093
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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-Rule MF_01398

Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP-Rule 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-Rule 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-Rule MF_01398
PRO_0000368378

Regions

Transmembrane7 – 2923Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q0BJL9 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: D5926C2280139075

FASTA15617,078
        10         20         30         40         50         60 
MNLNATLFAQ MVVFLVLAWF TMKFVWPPLI NALDERSKKI ADGLAAAEKG KAELDAAHKR 

        70         80         90        100        110        120 
VDQELAQARN DGQQRIADAE KRAQAVAEEI KANAQAEAAR IVAQAKAEAE QQIVKAREAL 

       130        140        150 
RGEVASLAVK GAEQILKREV DQTAHAQLLN QLKAEL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000440 Genomic DNA. Translation: ABI85654.1.
RefSeqYP_771988.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BJL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339670.Bamb_0093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI85654; ABI85654; Bamb_0093.
GeneID4311221.
KEGGbam:Bamb_0093.
PATRIC19015628. VBIBurAmb61564_0142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0711.
HOGENOMHOG000015378.
KOK02109.
OMAWPPLVKA.
OrthoDBEOG6DNTDK.
ProtClustDBPRK05759.

Enzyme and pathway databases

BioCycBAMB339670:GH48-95-MONOMER.

Family and domain databases

HAMAPMF_01398. ATP_synth_b_bact.
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_BURCM
AccessionPrimary (citable) accession number: Q0BJL9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 49 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