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Protein

ATP synthase subunit c

Gene

atpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei61Reversibly protonated during proton transport1

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
  • proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-MONOMER.
ECOL316407:JW3715-MONOMER.
MetaCyc:ATPE-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 c
Alternative name(s):
ATP synthase F(0) sector subunit c
Dicyclohexylcarbodiimide-binding protein
F-type ATPase subunit c
Short name:
F-ATPase subunit c
Lipid-binding protein
Gene namesi
Name:atpE
Synonyms:papH, uncE
Ordered Locus Names:b3737, JW3715
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10102. atpE.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10Periplasmic10
Transmembranei11 – 31HelicalAdd BLAST21
Topological domaini32 – 52CytoplasmicAdd BLAST21
Transmembranei53 – 73HelicalAdd BLAST21
Topological domaini74 – 79Periplasmic6

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • plasma membrane Source: UniProtKB-SubCell
  • 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23G → D in uncE429; unable to assemble in the membrane. 1 Publication1
Mutagenesisi28I → V in DC1; has a functional F0 as well as F1 part. However, the ATPase activity is inhibited. 1 Publication1
Mutagenesisi31L → F in uncE408 and uncE463; unable to assemble in the membrane. 1 Publication1
Mutagenesisi61D → G in DG 7/1; contains an enzymatically active F1 component, but no functional F0 component. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001121441 – 79ATP synthase subunit cAdd BLAST79

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionineBy similarity1

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiP68699.
PRIDEiP68699.

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). 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.1 Publication

Protein-protein interaction databases

DIPiDIP-2198N.
IntActiP68699. 3 interactors.
MINTiMINT-8087956.
STRINGi511145.b3737.

Structurei

Secondary structure

179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 39Combined sources38
Beta strandi44 – 46Combined sources3
Helixi47 – 78Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A91NMR-A1-79[»]
1ATYNMR-A1-79[»]
1C0VNMR-A1-79[»]
1C17NMR-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1C99NMR-A1-79[»]
1IJPNMR-A1-79[»]
1J7Fmodel-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1L6TNMR-A1-79[»]
1QO1X-ray3.90K/L/M/N/O/P/Q/R/S/T1-79[»]
4UTQelectron microscopy8.00Z1-79[»]
ProteinModelPortaliP68699.
SMRiP68699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68699.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636. LUCA.
HOGENOMiHOG000235244.
InParanoidiP68699.
KOiK02110.
OMAiMDLLYIA.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact. 1 hit.
InterProiIPR005953. ATP_synth_csu_bac/chlpt.
IPR000454. ATP_synth_F0_csu.
IPR020537. ATP_synth_F0_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P68699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR
60 70
TQFFIVMGLV DAIPMIAVGL GLYVMFAVA
Length:79
Mass (Da):8,256
Last modified:July 21, 1986 - v1
Checksum:i0F595A69D8AD1F9E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76F → S in CAA23591 (PubMed:6266400).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01594 Genomic DNA. Translation: AAA24732.1.
V00310 Genomic DNA. Translation: CAA23591.1.
M25464 Genomic DNA. Translation: AAA83870.1.
M12214 Genomic DNA. Translation: AAA23668.1.
V00266 Genomic DNA. Translation: CAA23522.1.
V00264 Genomic DNA. Translation: CAA23515.1.
V01506 Genomic DNA. Translation: CAA24752.1.
X01631 Genomic DNA. Translation: CAA25777.1.
L10328 Genomic DNA. Translation: AAA62089.1.
U00096 Genomic DNA. Translation: AAC76760.1.
AP009048 Genomic DNA. Translation: BAE77551.1.
PIRiB93732. LWECA.
RefSeqiNP_418193.1. NC_000913.3.
WP_000429386.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.
GeneIDi5549087.
948253.
KEGGiecj:JW3715.
eco:b3737.
PATRICi32122971. VBIEscCol129921_3861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01594 Genomic DNA. Translation: AAA24732.1.
V00310 Genomic DNA. Translation: CAA23591.1.
M25464 Genomic DNA. Translation: AAA83870.1.
M12214 Genomic DNA. Translation: AAA23668.1.
V00266 Genomic DNA. Translation: CAA23522.1.
V00264 Genomic DNA. Translation: CAA23515.1.
V01506 Genomic DNA. Translation: CAA24752.1.
X01631 Genomic DNA. Translation: CAA25777.1.
L10328 Genomic DNA. Translation: AAA62089.1.
U00096 Genomic DNA. Translation: AAC76760.1.
AP009048 Genomic DNA. Translation: BAE77551.1.
PIRiB93732. LWECA.
RefSeqiNP_418193.1. NC_000913.3.
WP_000429386.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A91NMR-A1-79[»]
1ATYNMR-A1-79[»]
1C0VNMR-A1-79[»]
1C17NMR-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1C99NMR-A1-79[»]
1IJPNMR-A1-79[»]
1J7Fmodel-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1L6TNMR-A1-79[»]
1QO1X-ray3.90K/L/M/N/O/P/Q/R/S/T1-79[»]
4UTQelectron microscopy8.00Z1-79[»]
ProteinModelPortaliP68699.
SMRiP68699.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2198N.
IntActiP68699. 3 interactors.
MINTiMINT-8087956.
STRINGi511145.b3737.

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.

Proteomic databases

PaxDbiP68699.
PRIDEiP68699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.
GeneIDi5549087.
948253.
KEGGiecj:JW3715.
eco:b3737.
PATRICi32122971. VBIEscCol129921_3861.

Organism-specific databases

EchoBASEiEB0100.
EcoGeneiEG10102. atpE.

Phylogenomic databases

eggNOGiCOG0636. LUCA.
HOGENOMiHOG000235244.
InParanoidiP68699.
KOiK02110.
OMAiMDLLYIA.

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-MONOMER.
ECOL316407:JW3715-MONOMER.
MetaCyc:ATPE-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68699.
PROiP68699.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact. 1 hit.
InterProiIPR005953. ATP_synth_csu_bac/chlpt.
IPR000454. ATP_synth_F0_csu.
IPR020537. ATP_synth_F0_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATPL_ECOLI
AccessioniPrimary (citable) accession number: P68699
Secondary accession number(s): P00844, Q2M855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Dicyclohexylcarbodiimide (DCDD) binding to the reversibly protonated aspartate residue inhibits ATPase in vitro.
In this organism c-rings of between c8 and c(12) can be isolated in vivo following experimental manipulations, however only c8 and c9, in addition to c(10), are partially functional.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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 one 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.