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Reviewed, UniProtKB/Swiss-Prot A0AFQ9 (ATPA1_LISW6)

Last modified November 3, 2009. Version 28. 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: lwe0423
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498ATP synthase subunit alpha 1 HAMAP MF_01346
PRO_0000339037

Regions

Nucleotide binding164 – 1718ATP Potential

Sites

Site3571Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0AFQ9-1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 18E70B92C1EA52B1

FASTA49855,135
        10         20         30         40         50         60 
MKTIQFDMNK YETHVDLEYL KEHGRVEKIS DGVIFCSGLE NAALHQAVLI DERHRGVILE 

        70         80         90        100        110        120 
LNEEFVGIGL IDKTSDILEG MNVSVTDHFI EVNLFDDMAG RIIDTTGKML YEESEEQPTS 

       130        140        150        160        170        180 
SSPLFRVTPE IMTIDSVTRP LNTGLAVIDS ITPIGRGQRQ LILGNRQSGK TQIAVDTIIN 

       190        200        210        220        230        240 
QHDQNVHCIY VAIGLKAAYI AEVIETLRNH DALKYSTVVA TAASDSLTAQ YLTPYAGMAV 

       250        260        270        280        290        300 
AEALREQGKD VLIIFDDLTK HADAYRAITL LFNRPPGREA YPGDSFYIHS SLLERAVQMN 

       310        320        330        340        350        360 
PEHGGGSITA LPMIETLSDD VTAYIPTNVI SITDGQLFLK SDLFNRGQKP AVDVGVSVSR 

       370        380        390        400        410        420 
IGGDAQHPII RKLSKNLTLI LSQFEELKEL LDFGNGLDEG SMKMVTDGRI LTELFKQKIL 

       430        440        450        460        470        480 
SPLSVTDLIV ILYAFQNGFL TKVPPAKIES FKGLLLEKAH ARNDFIAFSN DIKDISELSD 

       490 
AHTKMLEEII QEVGRLFS 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed: 16936040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM263198 Genomic DNA. Translation: CAK19841.1.
RefSeqYP_848624.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0AFQ9.

Genome annotation databases

GeneID4464983.
GenomeReviewsGene locus lwe0423 in contig AM263198_GR.
KEGGlwe:lwe0423.
NMPDRfig|386043.6.peg.402.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADMAGRII.

Family and domain databases

HAMAPMF_01346.
[Tree]
InterProIPR005294. ATPase_F1-cplx_asu.
IPR017458. ATPase_F1-cplx_asu_C.
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.
[Graphical view]
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA1_LISW6
AccessionPrimary (citable) accession number: A0AFQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 28, 2006
Last modified: November 3, 2009
This is version 28 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