Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit c, chloroplastic

Gene

atpH

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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.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

Miscellaneous

In plastids the F-type ATPase is also known as CF1CF0.
Dicyclohexylcarbodiimide (DCDD) inhibits ATPase.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei61Reversibly protonated during proton transportUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit c, chloroplasticUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit cUniRule annotation
ATPase subunit IIIUniRule annotation
F-type ATPase subunit cUniRule annotation
Short name:
F-ATPase subunit cUniRule annotation
Lipid-binding proteinUniRule annotation
Gene namesi
Name:atpHUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
Proteomesi

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei3 – 23HelicalUniRule annotationAdd BLAST21
Transmembranei57 – 77HelicalUniRule annotationAdd BLAST21

Keywords - Cellular componenti

CF(0), Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001121841 – 82ATP synthase subunit c, chloroplasticAdd BLAST82

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiQ37304

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

STRINGi3055.DAA00954

Structurei

3D structure databases

ProteinModelPortaliQ37304
SMRiQ37304
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232 Eukaryota
COG0636 LUCA
InParanoidiQ37304
KOiK02110

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.

Q37304-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPIVAATSV VSAGLAVGLA AIGPGMGQGT AAGYAVEGIA RQPEAEGKIR
60 70 80
GALLLSFAFM ESLTIYGLVV ALALLFANPF AG
Length:82
Mass (Da):8,093
Last modified:November 1, 1996 - v1
Checksum:iBFDC3BAF43E96A45
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti8T → A in strain: CC-503. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90559 Genomic DNA Translation: CAA62149.1
FJ423446 Genomic DNA Translation: ACJ50140.1
BK000554 Genomic DNA Translation: DAA00954.1
PIRiS58349
RefSeqiNP_958409.1, NC_005353.1

Genome annotation databases

EnsemblPlantsiDAA00954; DAA00954; DAA00954
GeneIDi2717044
GrameneiDAA00954; DAA00954; DAA00954
KEGGicre:ChreCp053

Entry informationi

Entry nameiATPH_CHLRE
AccessioniPrimary (citable) accession number: Q37304
Secondary accession number(s): B7U1J3, Q9T2G4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health