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Protein

ATP synthase subunit c

Gene

atpE

Organism
Prochlorococcus marinus (strain AS9601)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 611Reversibly protonated during proton transportUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciPMAR146891:GH90-1688-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit cUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit cUniRule annotation
F-type ATPase subunit cUniRule annotation
Short name:
F-ATPase subunit cUniRule annotation
Lipid-binding proteinUniRule annotation
Gene namesi
Name:atpEUniRule annotation
Synonyms:atpHUniRule annotation
Ordered Locus Names:A9601_16571
OrganismiProchlorococcus marinus (strain AS9601)
Taxonomic identifieri146891 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
Proteomesi
  • UP000002590 Componenti: Chromosome

Subcellular locationi

  • Cellular thylakoid membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2721HelicalUniRule annotationAdd
BLAST
Transmembranei57 – 7721HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181ATP synthase subunit cPRO_0000365911Add
BLAST

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 four main subunits: a1, b1, b'1 and c(10-14). 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, b and b' chains.UniRule annotation

Protein-protein interaction databases

STRINGi146891.A9601_16571.

Structurei

3D structure databases

ProteinModelPortaliA2BT29.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105VH4. Bacteria.
COG0636. LUCA.
HOGENOMiHOG000235245.
KOiK02110.
OMAiCSIITAG.
OrthoDBiEOG68H8G3.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2BT29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSITSAASV VAAGLAVGLG AIGPGLGQGN AAQGAVEGIA RQPEAEGKIR
60 70 80
GTLLLSFAFM ESLTIYGLVV ALVLLFANPF S
Length:81
Mass (Da):8,018
Last modified:February 20, 2007 - v1
Checksum:i48CD87D75C9888DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000551 Genomic DNA. Translation: ABM70940.1.
RefSeqiWP_002805169.1. NC_008816.1.

Genome annotation databases

EnsemblBacteriaiABM70940; ABM70940; A9601_16571.
KEGGipmb:A9601_16571.
PATRICi22984851. VBIProMar75723_1669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000551 Genomic DNA. Translation: ABM70940.1.
RefSeqiWP_002805169.1. NC_008816.1.

3D structure databases

ProteinModelPortaliA2BT29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi146891.A9601_16571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM70940; ABM70940; A9601_16571.
KEGGipmb:A9601_16571.
PATRICi22984851. VBIProMar75723_1669.

Phylogenomic databases

eggNOGiENOG4105VH4. Bacteria.
COG0636. LUCA.
HOGENOMiHOG000235245.
KOiK02110.
OMAiCSIITAG.
OrthoDBiEOG68H8G3.

Enzyme and pathway databases

BioCyciPMAR146891:GH90-1688-MONOMER.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AS9601.

Entry informationi

Entry nameiATPL_PROMS
AccessioniPrimary (citable) accession number: A2BT29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: February 20, 2007
Last modified: November 11, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.