UniProtKB - P68699 (ATPL_ECOLI)
Protein
ATP synthase subunit c
Gene
atpE
Organism
Escherichia coli (strain K12)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 61 | Reversibly protonated during proton transport | 1 |
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
- ATP synthesis coupled proton transport Source: GO_Central
Keywordsi
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Ligand | Lipid-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:ATPE-MONOMER MetaCyc:ATPE-MONOMER |
Protein family/group databases
TCDBi | 3.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 cAlternative 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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 10 | Periplasmic | 10 | |
Transmembranei | 11 – 31 | HelicalAdd BLAST | 21 | |
Topological domaini | 32 – 52 | CytoplasmicAdd BLAST | 21 | |
Transmembranei | 53 – 73 | HelicalAdd BLAST | 21 | |
Topological domaini | 74 – 79 | Periplasmic | 6 |
GO - Cellular componenti
- integral component of membrane Source: UniProtKB-KW
- 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), MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 23 | G → D in uncE429; unable to assemble in the membrane. 1 Publication | 1 | |
Mutagenesisi | 28 | I → V in DC1; has a functional F0 as well as F1 part. However, the ATPase activity is inhibited. 1 Publication | 1 | |
Mutagenesisi | 31 | L → F in uncE408 and uncE463; unable to assemble in the membrane. 1 Publication | 1 | |
Mutagenesisi | 61 | D → G in DG 7/1; contains an enzymatically active F1 component, but no functional F0 component. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000112144 | 1 – 79 | ATP synthase subunit cAdd BLAST | 79 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-formylmethionineBy similarity | 1 |
Keywords - PTMi
FormylationProteomic databases
jPOSTi | P68699 |
PaxDbi | P68699 |
PRIDEi | P68699 |
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 PublicationProtein-protein interaction databases
BioGRIDi | 4262599, 52 interactors |
ComplexPortali | CPX-4022, ATP synthase complex |
DIPi | DIP-2198N |
IntActi | P68699, 3 interactors |
MINTi | P68699 |
STRINGi | 511145.b3737 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P68699 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P68699 |
Family & Domainsi
Sequence similaritiesi
Belongs to the ATPase C chain family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG5032S3K, Bacteria |
HOGENOMi | CLU_148047_1_0_6 |
InParanoidi | P68699 |
Family and domain databases
Gene3Di | 1.20.20.10, 1 hit |
HAMAPi | MF_01396, ATP_synth_c_bact, 1 hit |
InterProi | View protein in InterPro IPR005953, ATP_synth_csu_bac/chlpt IPR000454, ATP_synth_F0_csu IPR020537, ATP_synth_F0_csu_DDCD_BS IPR038662, ATP_synth_F0_csu_sf IPR002379, ATPase_proteolipid_c-like_dom IPR035921, F/V-ATP_Csub_sf |
Pfami | View protein in Pfam PF00137, ATP-synt_C, 1 hit |
PRINTSi | PR00124, ATPASEC |
SUPFAMi | SSF81333, SSF81333, 1 hit |
TIGRFAMsi | TIGR01260, ATP_synt_c, 1 hit |
PROSITEi | View protein in PROSITE PS00605, ATPASE_C, 1 hit |
i Sequence
Sequence statusi: Complete.
P68699-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR
60 70
TQFFIVMGLV DAIPMIAVGL GLYVMFAVA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 76 | F → S in CAA23591 (PubMed:6266400).Curated | 1 |
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 |
PIRi | B93732, LWECA |
RefSeqi | NP_418193.1, NC_000913.3 WP_000429386.1, NZ_STEB01000015.1 |
Genome annotation databases
EnsemblBacteriai | AAC76760; AAC76760; b3737 BAE77551; BAE77551; BAE77551 |
GeneIDi | 58461070 948253 |
KEGGi | ecj:JW3715 eco:b3737 |
PATRICi | fig|1411691.4.peg.2963 |
Similar proteinsi
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 |
PIRi | B93732, LWECA |
RefSeqi | NP_418193.1, NC_000913.3 WP_000429386.1, NZ_STEB01000015.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A91 | NMR | - | A | 1-79 | [»] | |
1ATY | NMR | - | A | 1-79 | [»] | |
1C0V | NMR | - | A | 1-79 | [»] | |
1C17 | NMR | - | A/B/C/D/E/F/G/H/I/J/K/L | 1-79 | [»] | |
1C99 | NMR | - | A | 1-79 | [»] | |
1IJP | NMR | - | A | 1-79 | [»] | |
1J7F | model | - | A/B/C/D/E/F/G/H/I/J/K/L | 1-79 | [»] | |
1L6T | NMR | - | A | 1-79 | [»] | |
1QO1 | X-ray | 3.90 | K/L/M/N/O/P/Q/R/S/T | 1-79 | [»] | |
4UTQ | electron microscopy | 8.00 | Z | 1-79 | [»] | |
5T4O | electron microscopy | 6.90 | M/N/O/P/Q/R/S/T/U/V | 1-79 | [»] | |
5T4P | electron microscopy | 7.77 | M/N/O/P/Q/R/S/T/U/V | 1-79 | [»] | |
5T4Q | electron microscopy | 8.53 | M/N/O/P/Q/R/S/T/U/V | 1-79 | [»] | |
6OQR | electron microscopy | 3.10 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6OQS | electron microscopy | 3.30 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6OQT | electron microscopy | 3.10 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6OQU | electron microscopy | 3.20 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6OQV | electron microscopy | 3.30 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6OQW | electron microscopy | 3.10 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6PQV | electron microscopy | 3.30 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6VWK | electron microscopy | 3.30 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6WNQ | electron microscopy | 3.40 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
6WNR | electron microscopy | 3.30 | I/J/L/M/N/O/P/Q/R/S | 1-79 | [»] | |
SMRi | P68699 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262599, 52 interactors |
ComplexPortali | CPX-4022, ATP synthase complex |
DIPi | DIP-2198N |
IntActi | P68699, 3 interactors |
MINTi | P68699 |
STRINGi | 511145.b3737 |
Protein family/group databases
TCDBi | 3.A.2.1.1, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily |
Proteomic databases
jPOSTi | P68699 |
PaxDbi | P68699 |
PRIDEi | P68699 |
Genome annotation databases
EnsemblBacteriai | AAC76760; AAC76760; b3737 BAE77551; BAE77551; BAE77551 |
GeneIDi | 58461070 948253 |
KEGGi | ecj:JW3715 eco:b3737 |
PATRICi | fig|1411691.4.peg.2963 |
Organism-specific databases
EchoBASEi | EB0100 |
Phylogenomic databases
eggNOGi | ENOG5032S3K, Bacteria |
HOGENOMi | CLU_148047_1_0_6 |
InParanoidi | P68699 |
Enzyme and pathway databases
BioCyci | EcoCyc:ATPE-MONOMER MetaCyc:ATPE-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P68699 |
PROi | PR:P68699 |
Family and domain databases
Gene3Di | 1.20.20.10, 1 hit |
HAMAPi | MF_01396, ATP_synth_c_bact, 1 hit |
InterProi | View protein in InterPro IPR005953, ATP_synth_csu_bac/chlpt IPR000454, ATP_synth_F0_csu IPR020537, ATP_synth_F0_csu_DDCD_BS IPR038662, ATP_synth_F0_csu_sf IPR002379, ATPase_proteolipid_c-like_dom IPR035921, F/V-ATP_Csub_sf |
Pfami | View protein in Pfam PF00137, ATP-synt_C, 1 hit |
PRINTSi | PR00124, ATPASEC |
SUPFAMi | SSF81333, SSF81333, 1 hit |
TIGRFAMsi | TIGR01260, ATP_synt_c, 1 hit |
PROSITEi | View protein in PROSITE PS00605, ATPASE_C, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ATPL_ECOLI | |
Accessioni | P68699Primary (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: | February 10, 2021 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families