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Protein

ATP synthase subunit b

Gene

atpF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation
Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei9 – 91Mutation prevents the formation of a functional proton pore, but has a small effect on the binding of F(1) to F(0)
Sitei131 – 1311Required for proton pore formation, as well as F(1) to F(0) binding

GO - Molecular functioni

  1. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
  2. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  1. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

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

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit bUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit bUniRule annotation
ATPase subunit IUniRule annotation
F-type ATPase subunit bUniRule annotation
Short name:
F-ATPase subunit bUniRule annotation
Gene namesi
Name:atpFUniRule annotation
Synonyms:papF, uncF
Ordered Locus Names:b3736, JW3714
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10103. atpF.

Subcellular locationi

Cell inner membrane UniRule annotation; Single-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. anchored component of membrane Source: EcoliWiki
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
  4. proton-transporting ATP synthase complex, coupling factor F(o) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(0), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156ATP synthase subunit bPRO_0000082371Add
BLAST

Proteomic databases

PaxDbiP0ABA0.
PRIDEiP0ABA0.

2D gel databases

SWISS-2DPAGEP0ABA0.

Expressioni

Gene expression databases

GenevestigatoriP0ABA0.

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

DIPiDIP-35994N.
IntActiP0ABA0. 2 interactions.
STRINGi511145.b3736.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2421Combined sources
Helixi26 – 338Combined sources
Helixi63 – 12058Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9UNMR-A1-34[»]
1L2PX-ray1.55A62-122[»]
2KHKNMR-A30-82[»]
ProteinModelPortaliP0ABA0.
SMRiP0ABA0. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABA0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase B chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0711.
HOGENOMiHOG000015378.
InParanoidiP0ABA0.
KOiK02109.
OMAiVMKQREE.
OrthoDBiEOG6DNTDK.
PhylomeDBiP0ABA0.

Family and domain databases

Gene3Di1.20.5.620. 1 hit.
HAMAPiMF_01398. ATP_synth_b_bact.
InterProiIPR028987. ATPase_B-like_membr.
IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
PfamiPF00430. ATP-synt_B. 1 hit.
[Graphical view]
SUPFAMiSSF81573. SSF81573. 1 hit.
TIGRFAMsiTIGR01144. ATP_synt_b. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ABA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA
60 70 80 90 100
HKDLDLAKAS ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK
110 120 130 140 150
IVAQAQAEIE AERKRAREEL RKQVAILAVA GAEKIIERSV DEAANSDIVD

KLVAEL
Length:156
Mass (Da):17,264
Last modified:July 21, 1986 - v1
Checksum:i51A93C8BEE9AD9DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331I → F in CAA23592. (PubMed:6277311)Curated
Sequence conflicti62 – 621T → N in AAA24741. (PubMed:7686882)Curated
Sequence conflicti72 – 721A → D in CAA23592. (PubMed:6277311)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD93732. LWECB.
RefSeqiNP_418192.1. NC_000913.3.
YP_491693.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76759; AAC76759; b3736.
BAE77552; BAE77552; BAE77552.
GeneIDi12933115.
948247.
KEGGiecj:Y75_p3432.
eco:b3736.
PATRICi32122969. VBIEscCol129921_3860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD93732. LWECB.
RefSeqiNP_418192.1. NC_000913.3.
YP_491693.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9UNMR-A1-34[»]
1L2PX-ray1.55A62-122[»]
2KHKNMR-A30-82[»]
ProteinModelPortaliP0ABA0.
SMRiP0ABA0. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35994N.
IntActiP0ABA0. 2 interactions.
STRINGi511145.b3736.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGEP0ABA0.

Proteomic databases

PaxDbiP0ABA0.
PRIDEiP0ABA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76759; AAC76759; b3736.
BAE77552; BAE77552; BAE77552.
GeneIDi12933115.
948247.
KEGGiecj:Y75_p3432.
eco:b3736.
PATRICi32122969. VBIEscCol129921_3860.

Organism-specific databases

EchoBASEiEB0101.
EcoGeneiEG10103. atpF.

Phylogenomic databases

eggNOGiCOG0711.
HOGENOMiHOG000015378.
InParanoidiP0ABA0.
KOiK02109.
OMAiVMKQREE.
OrthoDBiEOG6DNTDK.
PhylomeDBiP0ABA0.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0ABA0.
PROiP0ABA0.

Gene expression databases

GenevestigatoriP0ABA0.

Family and domain databases

Gene3Di1.20.5.620. 1 hit.
HAMAPiMF_01398. ATP_synth_b_bact.
InterProiIPR028987. ATPase_B-like_membr.
IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
PfamiPF00430. ATP-synt_B. 1 hit.
[Graphical view]
SUPFAMiSSF81573. SSF81573. 1 hit.
TIGRFAMsiTIGR01144. ATP_synt_b. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiATPF_ECOLI
AccessioniPrimary (citable) accession number: P0ABA0
Secondary accession number(s): P00859, Q2M854
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.