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Q07YM0 (ATPA1_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 alpha 1
EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha 1
F-ATPase subunit alpha 1
Gene names
Name:atpA1
Ordered Locus Names:Sfri_3056
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length517 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 – 517517ATP synthase subunit alpha 1 HAMAP MF_01346
PRO_0000339057

Regions

Nucleotide binding176 – 1838ATP By similarity

Sites

Site3691Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07YM0 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 6ABF3D63DC552315

FASTA51756,044
        10         20         30         40         50         60 
MKLAPDLLQA TFEQTFSILQ QARRSFSPQL QPREIGTITS IATGIAKVSG LPGVGFEEIL 

        70         80         90        100        110        120 
KFPSDIFGIA FNVDEDEIGA VLLGDYWHLQ AGDEVERCGH LVDVPVGEGL LGRIINPIGE 

       130        140        150        160        170        180 
PLDGKGRLIA SARLPIERPS PAIMNRAPVS VPLQTGIKVI DALIPVGLGQ RELILGDRQT 

       190        200        210        220        230        240 
GKTAIAVDTI LNQRDKNVLC VYCAIGQRAS GVAKVIATLH EQGALEYTVV VVTEGNDPPG 

       250        260        270        280        290        300 
LAYIAPYAAT SIAEYFMQQG RNVLIVYDDL THHARAYREL SLLLRRPPGR EAFPGDIFYI 

       310        320        330        340        350        360 
HSRLLERATH LSPNLGGGSL TALPIIETEA QDISAYIPTN LISITDGQIY LSPSLFELGV 

       370        380        390        400        410        420 
LPAIDVGKSV SRVGGKAQRA AYRAVASNLK LAYAQFEELE TFASFGARLD DSTLKTIDHG 

       430        440        450        460        470        480 
RRIRACLKQA ESTPISMIEQ IAVLLALTAN LFDEVPLDVM SQAEHAVRAA TADIPVEITA 

       490        500        510 
RLASTEKLTD EDRDGILQPV RDALAPFMHS QKRKEIT

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000447 Genomic DNA. Translation: ABI72894.1.
RefSeqYP_751733.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ07YM0.
SMRQ07YM0. Positions 24-507.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ07YM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4279960.
GenomeReviewsGene locus Sfri_3056 in contig CP000447_GR.
KEGGsfr:Sfri_3056.
NMPDRfig|318167.10.peg.2935.
PATRIC23500253. VBISheFri14343_3167.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0056.
HOGENOMHBG565875.
OMANVLCVYC.
ProtClustDBPRK13343.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR017710. Alt_ATPase_F1-cplx_asu.
IPR020003. 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.
TIGRFAMsTIGR03324. Alt_F1F0_F1_al. 1 hit.
TIGR00962. AtpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA1_SHEFN
AccessionPrimary (citable) accession number: Q07YM0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 31, 2006
Last modified: January 25, 2012
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

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