ATP synthase subunit beta - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P0ABB4 (ATPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from mutant phenotype PubMed 158358. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 158358. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
atpA	P0ABB0	7	EBI-368783,EBI-368707

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.10 Ref.11

Chain

2 – 460

459

ATP synthase subunit beta HAMAP-Rule MF_01347

PRO_0000144437

Regions

Nucleotide binding

150 – 157

ATP By similarity

Experimental info

Mutagenesis

157

T → A or C: Impairs ATPase activity.

Secondary structure

460

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABB4 [UniParc].

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

FASTA

460

50,325

        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' referencesShow '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 277:1453-1474(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.

PIR

PWECB. A93742.

RefSeq

NP_418188.1. NC_000913.2.
YP_491697.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8S	X-ray	4.40	D/E/F	1-460	[»]
3OAA	X-ray	3.26	D/E/F/L/M/N/T/U/V/b/c/d	2-460	[»]

ProteinModelPortal

P0ABB4.

SMR

P0ABB4. Positions 3-460.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31846N.

IntAct

P0ABB4. 27 interactions.

MINT

MINT-1251407.

STRING

511145.b3732.

Protein family/group databases

TCDB

3.A.2.1.1. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

2D gel databases

SWISS-2DPAGE

P0ABB4.

Proteomic databases

PaxDb

P0ABB4.

PRIDE

P0ABB4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76755; AAC76755; b3732.
BAE77556; BAE77556; BAE77556.

GeneID

12932182.
948244.

KEGG

ecj:Y75_p3436.
eco:b3732.

PATRIC

32122961. VBIEscCol129921_3856.

Organism-specific databases

EchoBASE

EB0099.

EcoGene

EG10101. atpD.

Phylogenomic databases

eggNOG

COG0055.

HOGENOM

HOG000009605.

K02112.

OMA

NNIAKGH.

ProtClustDB

PRK09280.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0ABB4.

Family and domain databases

Gene3D

1.10.1140.10. 1 hit.

HAMAP

MF_01347. ATP_synth_beta_bact.

InterPro

IPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
[Graphical view]

PANTHER

PTHR15184:SF8. PTHR15184:SF8. 1 hit.

Pfam

PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.

TIGRFAMs

TIGR01039. atpD. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABB4.

Entry information

Entry name

ATPB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents