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Protein

ATP synthase subunit c, sodium ion specific

Gene

atpE

Organism
Ilyobacter tartaricus
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 sodium 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 sodium translocation.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 11 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei65Reversibly binds sodium during transport1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit c, sodium ion specific
Alternative name(s):
ATP synthase F(0) sector subunit c
F-type ATPase subunit c
Short name:
F-ATPase subunit c
Lipid-binding protein
Gene namesi
Name:atpE
OrganismiIlyobacter tartaricus
Taxonomic identifieri167644 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeIlyobacter

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8Periplasmic8
Transmembranei9 – 29HelicalSequence analysisAdd BLAST21
Topological domaini30 – 67CytoplasmicAdd BLAST38
Transmembranei68 – 88HelicalSequence analysisAdd BLAST21
Topological domaini89Periplasmic1

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003658911 – 89ATP synthase subunit c, sodium ion specificAdd BLAST89

Interactioni

Subunit structurei

F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane sodium channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(11). 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

Structurei

Secondary structure

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 21Combined sources19
Helixi22 – 25Combined sources4
Helixi26 – 45Combined sources20
Helixi47 – 49Combined sources3
Helixi50 – 80Combined sources31
Turni85 – 87Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YCEX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v1-89[»]
2WGMX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v1-89[»]
ProteinModelPortaliQ8KRV3.
SMRiQ8KRV3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KRV3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

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.

Q8KRV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMLFAKTVV LAASAVGAGT AMIAGIGPGV GQGYAAGKAV ESVARQPEAK
60 70 80
GDIISTMVLG QAVAESTGIY SLVIALILLY ANPFVGLLG
Length:89
Mass (Da):8,795
Last modified:October 1, 2002 - v1
Checksum:iBC23BE5DC1FD76C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF522463 Genomic DNA. Translation: AAM94908.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF522463 Genomic DNA. Translation: AAM94908.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YCEX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v1-89[»]
2WGMX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v1-89[»]
ProteinModelPortaliQ8KRV3.
SMRiQ8KRV3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KRV3.

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_ILYTA
AccessioniPrimary (citable) accession number: Q8KRV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 1, 2002
Last modified: March 15, 2017
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The ATPase of I.tartaricus is of special interest because it uses sodium ions instead of protons as the physiological coupling ion.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.