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P0ABB4 (ATPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit beta

EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit beta
F-ATPase subunit beta
Gene names
Name:atpD
Synonyms:papB, uncD
Ordered Locus Names:b3732, JW3710
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. HAMAP-Rule MF_01347

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347

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.

Subcellular location

Cell inner membrane; Peripheral membrane protein HAMAP-Rule MF_01347.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

atpAP0ABB010EBI-368783,EBI-368707

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.11
Chain2 – 460459ATP synthase subunit beta HAMAP-Rule MF_01347
PRO_0000144437

Regions

Nucleotide binding150 – 1578ATP By similarity

Experimental info

Mutagenesis1571T → A or C: Impairs ATPase activity.

Secondary structure

............................................................................ 460
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABB4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 18DB33154B1AE6FE

FASTA46050,325
        10         20         30         40         50         60 
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG IVRTIAMGSS 

        70         80         90        100        110        120 
DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG EIGEEERWAI HRAAPSYEEL 

       130        140        150        160        170        180 
SNSQELLETG IKVIDLMCPF AKGGKVGLFG GAGVGKTVNM MELIRNIAIE HSGYSVFAGV 

       190        200        210        220        230        240 
GERTREGNDF YHEMTDSNVI DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL 

       250        260        270        280        290        300 
FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP 

       310        320        330        340        350        360 
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV GQEHYDTARG 

       370        380        390        400        410        420 
VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF LSQPFFVAEV FTGSPGKYVS 

       430        440        450        460 
LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI EEAVEKAKKL 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
Walker J.E., Gay N.J., Saraste M., Eberle A.N.
Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase."
Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.
Nucleic Acids Res. 9:5287-5296(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
Kanazawa H., Futai M.
Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Nucleotide sequence of the genes for beta and epsilon subunits of proton-translocating ATPase from Escherichia coli."
Kanazawa H., Kayano T., Kiyasu T., Futai M.
Biochem. Biophys. Res. Commun. 105:1257-1264(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli."
Kanazawa H., Kayano T., Mabuchi K., Futai M.
Biochem. Biophys. Res. Commun. 103:604-612(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
[9]"Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP."
Wise J.G., Hicke B.J., Boyer P.D.
FEBS Lett. 223:395-401(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 325-359.
[10]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
Strain: K12 / EMG2.
[11]Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
Submitted (FEB-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[12]"Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase."
Iwamoto A., Omote H., Hanada H., Tomioka N., Itai A., Maeda M., Futai M.
J. Biol. Chem. 266:16350-16355(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[14]"Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by X-ray crystallography."
Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.
Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01631 Genomic DNA. Translation: CAA25782.1.
V00267 Genomic DNA. Translation: CAA23527.1.
M25464 Genomic DNA. Translation: AAA83875.1.
J01594 Genomic DNA. Translation: AAA24737.1.
V00311 Genomic DNA. Translation: CAA23594.1.
V00312 Genomic DNA. Translation: CAA23598.1.
L10328 Genomic DNA. Translation: AAA62084.1.
U00096 Genomic DNA. Translation: AAC76755.1.
AP009048 Genomic DNA. Translation: BAE77556.1.
PIRPWECB. A93742.
RefSeqNP_418188.1. NC_000913.3.
YP_491697.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40D/E/F1-460[»]
3OAAX-ray3.26D/E/F/L/M/N/T/U/V/b/c/d2-460[»]
ProteinModelPortalP0ABB4.
SMRP0ABB4. Positions 3-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31846N.
IntActP0ABB4. 31 interactions.
MINTMINT-1251407.
STRING511145.b3732.

Protein family/group databases

TCDB3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGEP0ABB4.

Proteomic databases

PaxDbP0ABB4.
PRIDEP0ABB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76755; AAC76755; b3732.
BAE77556; BAE77556; BAE77556.
GeneID12932182.
948244.
KEGGecj:Y75_p3436.
eco:b3732.
PATRIC32122961. VBIEscCol129921_3856.

Organism-specific databases

EchoBASEEB0099.
EcoGeneEG10101. atpD.

Phylogenomic databases

eggNOGCOG0055.
HOGENOMHOG000009605.
KOK02112.
OMAEPYAKGG.
OrthoDBEOG6HQSP3.
PhylomeDBP0ABB4.
ProtClustDBPRK09280.

Enzyme and pathway databases

BioCycEcoCyc:ATPD-MONOMER.
ECOL316407:JW3710-MONOMER.
MetaCyc:ATPD-MONOMER.

Gene expression databases

GenevestigatorP0ABB4.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01347. ATP_synth_beta_bact.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABB4.
PROP0ABB4.

Entry information

Entry nameATPB_ECOLI
AccessionPrimary (citable) accession number: P0ABB4
Secondary accession number(s): P00824, Q2M850
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 88 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene