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P0ABB1 (ATPA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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

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:c4660
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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-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.

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 HAMAP-Rule MF_01346
PRO_0000144327

Regions

Nucleotide binding169 – 1768ATP By similarity

Sites

Site3731Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P0ABB1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DD1F3859375E9103

FASTA51355,222
        10         20         30         40         50         60 
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG EMISLPGNRY 

        70         80         90        100        110        120 
AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG RGLLGRVVNT LGAPIDGKGP 

       130        140        150        160        170        180 
LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY KAVDSMIPIG RGQRELIIGD RQTGKTALAI 

       190        200        210        220        230        240 
DAIINQRDSG IKCIYVAIGQ KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY 

       250        260        270        280        290        300 
AGCAMGEYFR DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER 

       310        320        330        340        350        360 
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETNLF 

       370        380        390        400        410        420 
NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY RELAAFSQFA SDLDDATRKQ 

       430        440        450        460        470        480 
LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA AERGYLADVE LSKIGSFEAA LLAYVDRDHA 

       490        500        510 
PLMQEINQTG GYNDEIEGKL KGILDSFKAT QSW 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN83092.1.
RefSeqNP_756518.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0ABB1.
SMRP0ABB1. Positions 24-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c4660.

Proteomic databases

PRIDEP0ABB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN83092; AAN83092; c4660.
GeneID1040243.
KEGGecc:c4660.
PATRIC18287001. VBIEscCol75197_4374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000130111.
KOK02111.
OMAGNAQIKS.
OrthoDBEOG67X1S1.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycECOL199310:C4660-MONOMER.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR018538. HAS-barrel.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF09378. HAS-barrel. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA_ECOL6
AccessionPrimary (citable) accession number: P0ABB1
Secondary accession number(s): P00822, Q47249
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 73 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