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Protein

ATP synthase subunit c, sodium ion specific

Gene

atpE

Organism
Ilyobacter tartaricus
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 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.

Miscellaneous

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

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

3D structure databases

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
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.

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

Similar proteinsi

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
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
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: October 10, 2018
This is version 77 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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