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Q5FNY6 (ATPA2_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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 alpha 2
EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha 2
F-ATPase subunit alpha 2
Gene names
Name:atpA2
Ordered Locus Names:GOX2174
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity. HAMAP MF_01346

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 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; Peripheral membrane protein By similarity HAMAP MF_01346.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507ATP synthase subunit alpha 2 HAMAP MF_01346
PRO_0000238257

Regions

Nucleotide binding171 – 1788ATP By similarity

Sites

Site3641Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FNY6 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 3B2DF8901820387F

FASTA50753,720
        10         20         30         40         50         60 
MPDTDQAASW LASARSSLTD ISVGPRTDRT GRVEDIGDGI ALISGLPDAK LDELLSFGNG 

        70         80         90        100        110        120 
RYGFVHGLEE DSIGCILLNN EGTIEAGDAV QGTSGVVSVP VGPGLLGRVV DPLGRPLDGK 

       130        140        150        160        170        180 
GPVEAETWFP VERPAPAIID RELVTEPVQT GTLAIDTLFP IGRGQRELIV GDRATGKTTI 

       190        200        210        220        230        240 
AVDAILAQKS NDMICVYVAI GQKTSSVQRV IETIRTRGNP DRCIIVVARP AEAPGLCWIA 

       250        260        270        280        290        300 
PFAAMSMAEY FRDRGQHALL VIDDLSKHAA THREVSLLTG RPPGREAYPG DIFYVHARLL 

       310        320        330        340        350        360 
ERAAKLSAAK GGGSLTALPV AETEAGNLSA YIPTNLISIT DGQIVLNRTL FDQGQKPAVD 

       370        380        390        400        410        420 
VGVSVSRVGG AAQSPILRSS VGTLRLDYAQ FIELEAFTRF GGLPDTHVRQ QLARGACIRA 

       430        440        450        460        470        480 
TLRQGPHAPL DLLQEVALVT ASQNGLLDGV TAKNIRTIQS GLGDYLRSNA SEISTAIESG 

       490        500 
GVLSAEQKER FVACLRQYVE PRASAAS

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References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000009 Genomic DNA. Translation: AAW61910.1.
RefSeqYP_192566.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FNY6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3250493.
GenomeReviewsGene locus GOX2174 in contig CP000009_GR.
KEGGgox:GOX2174.
NMPDRfig|290633.1.peg.2111.
PATRIC32612290. VBIGluOxy81109_2481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG565875.
OMANVLCVYC.
ProtClustDBPRK13343.

Enzyme and pathway databases

BioCycGOXY290633:GOX2174-MONOMER.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR020003. ATPase_a/bsu_AS.
IPR005294. ATPase_F1-cplx_asu.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KOK02111.
PANTHERPTHR15184:SF3. ATPase_F1_a. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR00962. AtpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA2_GLUOX
AccessionPrimary (citable) accession number: Q5FNY6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 57 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

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