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Reviewed, UniProtKB/Swiss-Prot Q6LLG6 (ATPA1_PHOPR)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP synthase subunit alpha 1
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 1
    ATP synthase F1 sector subunit alpha 1
Gene names
Name: atpA1
Ordered Locus Names: PBPRA3606
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length513 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. HAMAP MF_01346

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 – 513513ATP synthase subunit alpha 1 HAMAP MF_01346
PRO_0000238318

Regions

Nucleotide binding169 – 1768ATP By similarity

Sites

Site3731Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LLG6-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7F3E4CAFF0E84A28

FASTA51355,433
        10         20         30         40         50         60 
MQLNSTEISA LIKQRIEKFN VASEARNEGT IVSVSDGIIR IHGLADVMQG EMIELPGGRF 

        70         80         90        100        110        120 
ALALNLERDS VGAVVMGPYA NLQEGMKVTG TGRILEVPVG PALLGRVVNT LGEPIDGKGP 

       130        140        150        160        170        180 
IETETFSPVE VIAPGVIERK SVDQPVQTGY KAVDSMIPIG RGQRELIIGD RQTGKTAMAI 

       190        200        210        220        230        240 
DAIINQKQSG IYSVYVAIGQ KASTIANVVR KLEEHGALDN TIVVVASASE AAALQYLAPY 

       250        260        270        280        290        300 
SGCAMGEYFR DRGEDALIVY DDLSKQAVAY RQISLLLKRP PGREAFPGDV FYLHSRLLER 

       310        320        330        340        350        360 
ASRVSENYVE KFTNGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLQTELF 

       370        380        390        400        410        420 
NAGIRPAVDP GISVSRVGGS AQTKIIKKLS GGIRTALAQY RELAAFAQFS SDLDEATKKQ 

       430        440        450        460        470        480 
LDHGQKVTEL MKQKQYAPMS VFEQAVVIFS AERGYLVDVE LAKLADFEAA LLSYAKGQSA 

       490        500        510 
ELVSQIDETG AWNSEIEAQF VKLVEDFKAT QTW 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed: 15746425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378674 Genomic DNA. Translation: CAG21862.1.
RefSeqYP_131664.1.

3D structure databases

SMRQ6LLG6. Positions 24-510.
ModBaseSearch...

Genome annotation databases

GeneID3124674.
KEGGppr:PBPRA3606.
NMPDRfig|298386.1.peg.5782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG565875.
OMAEVVTELM.
PhylomeDBQ6LLG6.

Enzyme and pathway databases

BioCycPPRO298386:PBPRA3606-MONOMER.
BRENDA3.6.3.14. 263915.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR005294. ATPase_F1-cplx_asu.
IPR017458. ATPase_F1-cplx_asu_C.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR020003. ATPase_F1/V1/A1_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
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]
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA1_PHOPR
AccessionPrimary (citable) accession number: Q6LLG6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents