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Protein

ATP synthase subunit c

Gene

atpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

BioGridi4262599, 52 interactors
DIPiDIP-2198N
IntActiP68699, 3 interactors
MINTiP68699
STRINGi316385.ECDH10B_3924

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
OMAiNIATVGY

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
IPR038662 ATP_synth_F0_csu_sf
IPR002379 ATPase_proteolipid_c-like_dom
IPR035921 F/V-ATP_Csub_sf
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
GeneIDi34151810
948253
KEGGiecj:JW3715
eco:b3737
PATRICifig|1411691.4.peg.2963

Similar proteinsi

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: April 25, 2018
This is version 119 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

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