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A9CK01 (ATPF_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Atu0717
ORF Names:AGR_C_1301
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970)
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length161 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 – 161161ATP synthase subunit b HAMAP MF_01398
PRO_0000368301

Regions

Transmembrane3 – 2321Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A9CK01 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: E163A70100086FEB

FASTA16117,448
        10         20         30         40         50         60 
MAFDASFFAL VGLVLFFVLI AYLKVPGMLS KSLDERAQNI QDELAEAKRL REEAQHLLAE 

        70         80         90        100        110        120 
YQRKRKEAEA EAAGIVAAAE REAAALTEEA KQKTEEFVAR RTALSEQKIK QAEEDAIGAV 

       130        140        150        160 
RAAAVDIAIA ASEKLLAEKT TAAAKAKLFA ATIGEVKSKL N 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK86527.1.
PIRAG2664.
F97446.
RefSeqNP_353742.1. NC_003062.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA9CK01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1132755.
GenomeReviewsGene locus Atu0717 in contig AE007869_GR.
KEGGatu:Atu0717.
PATRIC20811143. VBIAgrTum91616_0715.

Phylogenomic databases

eggNOGCOG0711.
HOGENOMHBG692690.
OMAAEDQIAS.
ProtClustDBPRK09173.

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 nameATPF_AGRT5
AccessionPrimary (citable) accession number: A9CK01
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 31 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