ATP synthase subunit b - Escherichia coli (strain K12)

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P0ABA0 (ATPF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
ATP synthase subunit b

Alternative name(s):
ATP synthase F(0) sector subunit b
ATPase subunit I
F-type ATPase subunit b
Short name=F-ATPase subunit b

Gene names

Name:	atpF
Synonyms:	papF, uncF
Ordered Locus Names:	b3736, JW3714

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	F₁F₀ ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F₁ containing the extramembraneous catalytic core and F₀ containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F₁ is coupled via a rotary mechanism of the central stalk subunits to proton translocation By similarity. Ref.11 Component of the F₀ channel, it forms part of the peripheral stalk, linking F₁ to F₀ By similarity. Ref.11
Subunit structure	F-type ATPases have 2 components, F₁ - the catalytic core - and F₀ - the membrane proton channel. F₁ has five subunits: alpha₃, beta₃, gamma₁, delta₁, epsilon₁. F₀ has three main subunits: a₁, b₂ and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F₁ is attached to F₀ 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. Ref.12
Subcellular location	Cell inner membrane; Single-pass membrane protein By similarity Ref.12.
Sequence similarities	Belongs to the ATPase B chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	anchored to membrane Inferred from direct assay PubMed 2863271. Source: EcoliWiki integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from mutant phenotype PubMed 6460031. Source: EcoliWiki
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from mutant phenotype PubMed 2863271. Source: EcoCyc proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 6460031. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

ATP synthase subunit b HAMAP-Rule MF_01398

PRO_0000082371

Regions

Transmembrane

11 – 31

Helical; Potential

Sites

Site

Mutation prevents the formation of a functional proton pore, but has a small effect on the binding of F(1) to F(0)

Site

131

Required for proton pore formation, as well as F(1) to F(0) binding

Experimental info

Sequence conflict

I → F in CAA23592. Ref.3

Sequence conflict

T → N in AAA24741. Ref.7

Sequence conflict

A → D in CAA23592. Ref.3

Secondary structure

156

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABA0 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 51A93C8BEE9AD9DF
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FASTA

156

17,264

        10         20         30         40         50         60 
MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA HKDLDLAKAS 

        70         80         90        100        110        120 
ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK IVAQAQAEIE AERKRAREEL 

       130        140        150 
RKQVAILAVA GAEKIIERSV DEAANSDIVD KLVAEL

« 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 promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase." Gay N.J., Walker J.E. Nucleic Acids Res. 9:3919-3926(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits." Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M. Biochem. Biophys. Res. Commun. 103:613-620(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli." Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K. Mol. Gen. Genet. 184:33-39(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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].
[6]	"Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis." Porter A.C.G., Kumamoto C., Aldape K., Simoni R.D. J. Biol. Chem. 260:8182-8187(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli." Mabuchi K., Kanazawa H., Kayano T., Futai M. Biochem. Biophys. Res. Commun. 102:172-179(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-156.
[11]	"Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85." McCormick K.A., Cain B.D. J. Bacteriol. 173:7240-7248(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. Strain: BL21-DE3.
[13]	"Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase." Dmitriev O., Jones P.C., Jiang W., Fillingame R.H. J. Biol. Chem. 274:15598-15604(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-34.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01594 Genomic DNA. Translation: AAA24733.1.
X01631 Genomic DNA. Translation: CAA25778.1.
V00264 Genomic DNA. Translation: CAA23516.1.
V00310 Genomic DNA. Translation: CAA23592.1.
V00266 Genomic DNA. Translation: CAA23523.1.
M25464 Genomic DNA. Translation: AAA83871.1.
M10422 Genomic DNA. Translation: AAA24741.1.
L10328 Genomic DNA. Translation: AAA62088.1.
U00096 Genomic DNA. Translation: AAC76759.1.
AP009048 Genomic DNA. Translation: BAE77552.1.
M12212 Unassigned DNA. Translation: AAA20043.1.

PIR

LWECB. D93732.

RefSeq

NP_418192.1. NC_000913.2.
YP_491693.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B9U	NMR	-	A	1-34	[»]
1L2P	X-ray	1.55	A	62-122	[»]
2KHK	NMR	-	A	30-82	[»]

ProteinModelPortal

P0ABA0.

SMR

P0ABA0. Positions 1-122.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35994N.

IntAct

P0ABA0. 2 interactions.

STRING

511145.b3736.

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

P0ABA0.

Proteomic databases

PaxDb

P0ABA0.

PRIDE

P0ABA0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76759; AAC76759; b3736.
BAE77552; BAE77552; BAE77552.

GeneID

12933115.
948247.

KEGG

ecj:Y75_p3432.
eco:b3736.

PATRIC

32122969. VBIEscCol129921_3860.

Organism-specific databases

EchoBASE

EB0101.

EcoGene

EG10103. atpF.

Phylogenomic databases

eggNOG

COG0711.

HOGENOM

HOG000015378.

K02109.

OMA

VLPKFQE.

ProtClustDB

PRK05759.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPF-MONOMER.
ECOL316407:JW3714-MONOMER.
MetaCyc:ATPF-MONOMER.

Gene expression databases

Genevestigator

P0ABA0.

Family and domain databases

HAMAP

MF_01398. ATP_synth_b_bact.

InterPro

IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]

Pfam

PF00430. ATP-synt_B. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01144. ATP_synt_b. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABA0.

Entry information

Entry name

ATPF_ECOLI

Accession

Primary (citable) accession number: P0ABA0
Secondary accession number(s): P00859, Q2M854

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

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