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Information on EC 7.2.2.6 - P-type K+ transporter

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EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
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This record set is specific for:
UNIPROT: P03959
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Word Map
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  • 7.2.2.6
  • kdpde
  • turgor
  • k+-limiting
  • info
  • ptsntr
  • k+-uptake
  • eintr
  • c-di-amp
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide
ATP
+
H2O
+
K+[side 1]
=
ADP
+
phosphate
+
K+[side 2]
+
+
=
+
+
Synonyms
kdpfabc, potassium atpase, kdpabc, pykpa1, k+-translocating kdp-atpase, k+-transporting atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine 5'-triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
-
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ATP hydrolase
-
-
-
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ATP phosphohydrolase
-
-
-
-
complex V (mitochondrial electron transport)
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-
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K+-translocating Kdp-ATPase
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-
-
-
KdpABC
-
-
-
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multi-subunit K+-transport ATPase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, K+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDPA_ECOLI
Escherichia coli (strain K12)
557
0
59189
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Durell, S.R.; Bakker, E.P.; Guy, H.R.
Does the KdpA subunit from the high affinity K+-translocating P-type KDP-ATPase have a structure similar to that of K+ channels?
Biophys. J.
78
188-199
2000
Mycobacterium tuberculosis, Clostridium acetobutylicum (O32327), Escherichia coli (P03959), Synechocystis sp. PCC 6803 (P73866), Alicyclobacillus acidocaldarius (Q9XE11)
Manually annotated by BRENDA team