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Q83AF7 (ATPA_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha

EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha
F-ATPase subunit alpha
Gene names
Name:atpA
Ordered Locus Names:CBU_1943
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_01346

Catalytic activity

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

Developmental stage

Detected in both the small cell variant (SCV) and in the large cell variant (LCV) stage (at protein level). LCVs are more metabolically active than SCVs. Ref.2

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515ATP synthase subunit alpha HAMAP-Rule MF_01346
PRO_0000238237

Regions

Nucleotide binding171 – 1788ATP By similarity

Sites

Site3751Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83AF7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0D03A74C4A72CFDB

FASTA51556,844
        10         20         30         40         50         60 
MSTQLRAAEI SDIIESRIEK FGIKAEERTE GTILNIKDGI VRVYGLRDVM FGEMVEFPEN 

        70         80         90        100        110        120 
TYGLAFNLER DSVGAVVMGP YEHLEEGMTA RCTGRILEVP VGEALLGRVV DGLGKPIDGK 

       130        140        150        160        170        180 
GPIDTSETSP IEKVAPGVIT RKSVDTSLPT GLKSIDAMVP IGRGQRELII GDRQTGKTAI 

       190        200        210        220        230        240 
AIDTIINQKH TGVKCIYVAI GQKQSSVAAV VRKLEEHGAM EHTIVVNASA SEAAALQYLA 

       250        260        270        280        290        300 
PYAGCTMGEY FRDRGQDALI VYDDLTKQAW AYRQISLLLR RPPGREAYPG DIFYLHSRLL 

       310        320        330        340        350        360 
ERAAHVNEAY VKEFTKGKVT GKTGSLTALP IIETQAGDVS AFIPTNVISI TDGQIYLDVN 

       370        380        390        400        410        420 
LFNAGIRPAI NAGLSVSRVG GAAQTKIIKK LIGGLRIALA QYRELEAFSQ FASDLDEATR 

       430        440        450        460        470        480 
KQLEHGQRVM EILKQPQYQP LSVGEMAIIW YVVNNNYLDQ VELKKVVDFE RSLLSFLRDQ 

       490        500        510 
HQDLLDEINK NPNYSEKIIE KIKAVVEEFV KTQSY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO91433.1.
RefSeqNP_820919.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83AF7.
SMRQ83AF7. Positions 19-512.
ModBaseSearch...

Protein-protein interaction databases

STRING227377.CBU_1943.

Proteomic databases

PRIDEQ83AF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO91433; AAO91433; CBU_1943.
GeneID1209856.
KEGGcbu:CBU_1943.
PATRIC17932625. VBICoxBur82552_1929.

Phylogenomic databases

eggNOGCOG0056.
HOGENOMHOG000130111.
KOK02111.
OMADSGRHAL.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1917-MONOMER.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005294. ATPase_F1-cplx_asu.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
PANTHERPTHR15184:SF3. PTHR15184:SF3. 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 nameATPA_COXBU
AccessionPrimary (citable) accession number: Q83AF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

SIMILARITY comments

Index of protein domains and families