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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.

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

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

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandLipid-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-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

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[»]
5T4Oelectron microscopy6.90M/N/O/P/Q/R/S/T/U/V1-79[»]
5T4Pelectron microscopy7.77M/N/O/P/Q/R/S/T/U/V1-79[»]
5T4Qelectron microscopy8.53M/N/O/P/Q/R/S/T/U/V1-79[»]
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.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact. 1 hit.
InterProiView protein in InterPro
IPR005953. ATP_synth_csu_bac/chlpt.
IPR000454. ATP_synth_F0_csu.
IPR020537. ATP_synth_F0_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
PANTHERiPTHR10031. PTHR10031. 1 hit.
PfamiView protein in Pfam
PF00137. ATP-synt_C. 1 hit.
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiView protein in PROSITE
PS00605. ATPASE_C. 1 hit.

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.
GeneIDi31869912.
948253.
KEGGiecj:JW3715.
eco:b3737.
PATRICifig|1411691.4.peg.2963.

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[»]
5T4Oelectron microscopy6.90M/N/O/P/Q/R/S/T/U/V1-79[»]
5T4Pelectron microscopy7.77M/N/O/P/Q/R/S/T/U/V1-79[»]
5T4Qelectron microscopy8.53M/N/O/P/Q/R/S/T/U/V1-79[»]
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.
GeneIDi31869912.
948253.
KEGGiecj:JW3715.
eco:b3737.
PATRICifig|1411691.4.peg.2963.

Organism-specific databases

EchoBASEiEB0100.
EcoGeneiEG10102. atpE.

Phylogenomic databases

eggNOGiCOG0636. LUCA.
HOGENOMiHOG000235244.
InParanoidiP68699.
KOiK02110.

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-MONOMER.
MetaCyc:ATPE-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68699.
PROiPR:P68699.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact. 1 hit.
InterProiView protein in InterPro
IPR005953. ATP_synth_csu_bac/chlpt.
IPR000454. ATP_synth_F0_csu.
IPR020537. ATP_synth_F0_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
PANTHERiPTHR10031. PTHR10031. 1 hit.
PfamiView protein in Pfam
PF00137. ATP-synt_C. 1 hit.
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiView protein in PROSITE
PS00605. ATPASE_C. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiATPL_ECOLI
AccessioniPrimary (citable) accession number: P68699
Secondary accession number(s): P00844, Q2M855
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 7, 2017
This is version 113 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

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.