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Reviewed, UniProtKB/Swiss-Prot O51876 (ATPF_BUCAP)

Last modified November 24, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP synthase subunit b
Alternative name(s):
    ATP synthase F(0) sector subunit b
    F-type ATPase subunit b
      Short name=F-ATPase subunit b
    ATPase subunit I
Gene names
Name: atpF
Ordered Locus Names: BUsg_004
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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

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 membrane; Single-pass membrane protein By similarity.

Sequence similarities

Belongs to the ATPase B chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163ATP synthase subunit b HAMAP MF_01398
PRO_0000082368

Regions

Transmembrane13 – 3321 Potential

Experimental info

Sequence conflict156 – 1638LSKDKKLI → FI Ref.1
Sequence conflict156 – 1638LSKDKKLI → FI Ref.2

Sequences

Sequence LengthMass (Da)Tools
O51876-1 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 3D4AE37A44255146

FASTA16319,075
        10         20         30         40         50         60 
MNLNATILGQ ALSFILFVWF CMKYIWPPII FAIETRQKNI EESLISLKKA EEELIIIQKK 

        70         80         90        100        110        120 
MNQIIQDSKE KASFIINEAN KKKSIILEDA KSIALEESKK IFLRNQLEID LKVMQVRKNL 

       130        140        150        160 
HKEIVDLSIL IAEKIIKDNI QKDQYKYSIK KLIVSLSKDK KLI 

« Hide

References

« Hide 'large scale' references
[1]"The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids): genetic analysis of the putative ATP operon."
Clark M.A., Baumann P.
Curr. Microbiol. 35:84-89(1997) [PubMed: 9216881] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon, gidA, and rho."
Clark M.A., Baumann L., Baumann P.
Curr. Microbiol. 36:158-163(1998) [PubMed: 9516544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AF008210 Genomic DNA. Translation: AAC38114.1.
AE013218 Genomic DNA. Translation: AAM67576.1.
RefSeqNP_660365.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1005824.
GenomeReviewsGene locus BUsg_004 in contig AE013218_GR.
KEGGbas:BUsg004.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO51876.
OMAASQRSSE

Enzyme and pathway databases

BioCycBAPH198804:BUSG004-MON.

Family and domain databases

HAMAPMF_01398.
[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_BUCAP
AccessionPrimary (citable) accession number: O51876
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 30, 2002
Last modified: November 24, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents