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Protein

ATP synthase subunit b

Gene

atpF

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciECOL199310:C4664-MONOMER

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
Ordered Locus Names:c4664
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei11 – 31HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000823731 – 156ATP synthase subunit bAdd BLAST156

Proteomic databases

PRIDEiP0ABA1

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

STRINGi199310.c4664

Structurei

3D structure databases

ProteinModelPortaliP0ABA1
SMRiP0ABA1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase B chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107Z6K Bacteria
COG0711 LUCA
HOGENOMiHOG000015378
KOiK02109
OMAiKFAWKPI

Family and domain databases

HAMAPiMF_01398 ATP_synth_b_bprime, 1 hit
InterProiView protein in InterPro
IPR028987 ATP_synth_B-like_membr_sf
IPR002146 ATP_synth_b/b'su_bac/chlpt
IPR005864 ATP_synth_F0_bsu_bac
PfamiView protein in Pfam
PF00430 ATP-synt_B, 1 hit
SUPFAMiSSF81573 SSF81573, 1 hit
TIGRFAMsiTIGR01144 ATP_synt_b, 1 hit

Sequencei

Sequence statusi: Complete.

P0ABA1-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA Translation: AAN83096.1
RefSeqiWP_001052219.1, NC_004431.1

Genome annotation databases

EnsemblBacteriaiAAN83096; AAN83096; c4664
KEGGiecc:c4664

Similar proteinsi

Entry informationi

Entry nameiATPF_ECOL6
AccessioniPrimary (citable) accession number: P0ABA1
Secondary accession number(s): P00859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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