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B0BZL2 (ATPA1_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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 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:AM1_0896
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length505 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 four main subunits: a1, b1, b'1 and c(9-12) By similarity.

Subcellular location

Cellular thylakoid 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 – 505505ATP synthase subunit alpha 1 HAMAP MF_01346
PRO_0000339009

Regions

Nucleotide binding170 – 1778ATP By similarity

Sites

Site3631Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BZL2 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: F52CB721F5B1259D

FASTA50554,611
        10         20         30         40         50         60 
MVSIRPDEIS NIIRQQIEQY DQQVKVDNVG TVLQVGDGIA RVYGLEQAMA GELLDFEDGT 

        70         80         90        100        110        120 
VGIALNLEED NVGAVLMGDG RDLQEGSTVR STGKIAQIPV GDALIGRVLD ALARPIDGKG 

       130        140        150        160        170        180 
DINTSETRLI ESPAPGIIER KSVYEPMQTG ITAIDSMVPI GRGQRELIIG DRQTGKTAVA 

       190        200        210        220        230        240 
IDTILNQKSE DVICVYVAIG QKASTVAQVV EVLRERGALD YTVVVAANAN DPATLQYLAP 

       250        260        270        280        290        300 
YTGAAIAEYF MYNGKHTLVI YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 

       310        320        330        340        350        360 
RAAKLSPELG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSSDLF NAGLRPAINA 

       370        380        390        400        410        420 
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDQATQNQ LARGARLREI 

       430        440        450        460        470        480 
LKQPQYSPLP VEEMVAVIYA GTNGYLDDVP TDKVTEFVQG MRDDLKANHA KYGELVRSEK 

       490        500 
KMGDEAEGIL KTAIADFKKS FMAAV

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW25938.1.
RefSeqYP_001515252.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0BZL2.
SMRB0BZL2. Positions 25-501.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0BZL2.

Proteomic databases

PRIDEB0BZL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5679722.
GenomeReviewsGene locus AM1_0896 in contig CP000828_GR.
KEGGamr:AM1_0896.
PATRIC20616286. VBIAcaMar40141_0792.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG565875.
OMAGSDRDIK.
PhylomeDBB0BZL2.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycAMAR329726:AM1_0896-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.
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 nameATPA1_ACAM1
AccessionPrimary (citable) accession number: B0BZL2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 37 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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