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Protein

Potassium-transporting ATPase KdpC subunit

Gene

kdpC

Organism
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) (Burkholderia phytofirmans)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.UniRule annotation

GO - Molecular functioni

Keywordsi

Biological processIon transport, Potassium transport, Transport
LigandATP-binding, Nucleotide-binding, Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-transporting ATPase KdpC subunitUniRule annotation
Alternative name(s):
ATP phosphohydrolase [potassium-transporting] C chainUniRule annotation
Potassium-binding and translocating subunit CUniRule annotation
Potassium-translocating ATPase C chainUniRule annotation
Gene namesi
Name:kdpCUniRule annotation
Ordered Locus Names:Bphyt_1310
OrganismiParaburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) (Burkholderia phytofirmans)
Taxonomic identifieri398527 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeParaburkholderia
Proteomesi
  • UP000001739 Componenti: Chromosome 1

Subcellular locationi

  • Cell inner membrane UniRule annotation; Single-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei7 – 27HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001147181 – 192Potassium-transporting ATPase KdpC subunitAdd BLAST192

Interactioni

Subunit structurei

The system is composed of three essential subunits: KdpA, KdpB and KdpC.UniRule annotation

Protein-protein interaction databases

STRINGi398527.Bphyt_1310

Structurei

3D structure databases

SMRiB2T2B4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the KdpC family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108R80 Bacteria
COG2156 LUCA
HOGENOMiHOG000244124
KOiK01548
OMAiFQVPRVA
OrthoDBiPOG091H0B4S

Family and domain databases

HAMAPiMF_00276 KdpC, 1 hit
InterProiView protein in InterPro
IPR003820 KdpC
PANTHERiPTHR30042 PTHR30042, 1 hit
PfamiView protein in Pfam
PF02669 KdpC, 1 hit
PIRSFiPIRSF001296 K_ATPase_KdpC, 1 hit
TIGRFAMsiTIGR00681 kdpC, 1 hit

Sequencei

Sequence statusi: Complete.

B2T2B4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNLFRPLIV IFAVLTAVTG LAYPAVMTAV GQAAFSDQAN GSMLEQDGKV
60 70 80 90 100
VGSKLIGQQF DAPQYFWGRL SATSPMPYNA QGSGGSNLGP TNPALLDEIK
110 120 130 140 150
GRIDALKTAG TDMSKPVPVD LVTSSGSGLD PEISPAAAAY QIERVAKARK
160 170 180 190
LAANDVQALV DRYTSGRQFG ILGEPRVNVL QLNLALDEMK HG
Length:192
Mass (Da):20,246
Last modified:July 1, 2008 - v1
Checksum:iC95A4B1D17966E1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001052 Genomic DNA Translation: ACD15725.1
RefSeqiWP_012432344.1, NC_010681.1

Genome annotation databases

EnsemblBacteriaiACD15725; ACD15725; Bphyt_1310
KEGGibpy:Bphyt_1310

Similar proteinsi

Entry informationi

Entry nameiKDPC_PARPJ
AccessioniPrimary (citable) accession number: B2T2B4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: April 25, 2018
This is version 60 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

Complete proteome, Reference proteome

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