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Protein

Potassium-transporting ATPase ATP-binding subunit

Gene

kdpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit is responsible for energy coupling to the transport system (PubMed:16354672).4 Publications

Catalytic activityi

ATP + H2O + K+(Out) = ADP + phosphate + K+(In).UniRule annotation1 Publication

Enzyme regulationi

ATPase activity is inhibited by vanadate, fluorescein isothiocyanate, N,N'-dicyclohexylcarbodiimide and N-ethylmaleimide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei307 – 30714-aspartylphosphate intermediateUniRule annotation
Binding sitei344 – 3441ATPUniRule annotationCombined sources1 Publication
Binding sitei348 – 3481ATPUniRule annotationCombined sources1 Publication
Binding sitei395 – 3951ATPUniRule annotationCombined sources1 Publication
Metal bindingi518 – 5181MagnesiumUniRule annotation
Metal bindingi522 – 5221MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi377 – 3848ATPUniRule annotationCombined sources1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • magnesium ion binding Source: UniProtKB-HAMAP
  • potassium-transporting ATPase activity Source: EcoliWiki

GO - Biological processi

  • potassium ion transport Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:KDPB-MONOMER.
ECOL316407:JW0685-MONOMER.
MetaCyc:KDPB-MONOMER.

Protein family/group databases

TCDBi3.A.3.7.1. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-transporting ATPase ATP-binding subunitUniRule annotation (EC:3.6.3.12UniRule annotation1 Publication)
Alternative name(s):
ATP phosphohydrolase [potassium-transporting] B chainUniRule annotation
Potassium-binding and translocating subunit BUniRule annotation
Potassium-translocating ATPase B chainUniRule annotation
Gene namesi
Name:kdpBUniRule annotation
Ordered Locus Names:b0697, JW0685
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10514. kdpB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicCuratedAdd
BLAST
Transmembranei34 – 5421HelicalUniRule annotationAdd
BLAST
Topological domaini55 – 617PeriplasmicCurated
Transmembranei62 – 8221HelicalUniRule annotationAdd
BLAST
Topological domaini83 – 218136CytoplasmicCuratedAdd
BLAST
Transmembranei219 – 23921HelicalUniRule annotationAdd
BLAST
Topological domaini240 – 25314PeriplasmicCuratedAdd
BLAST
Transmembranei254 – 27421HelicalUniRule annotationAdd
BLAST
Topological domaini275 – 587313CytoplasmicCuratedAdd
BLAST
Transmembranei588 – 60821HelicalUniRule annotationAdd
BLAST
Topological domaini609 – 6157PeriplasmicCurated
Transmembranei616 – 63621HelicalUniRule annotationAdd
BLAST
Topological domaini637 – 65519CytoplasmicCuratedAdd
BLAST
Transmembranei656 – 67621HelicalUniRule annotationAdd
BLAST
Topological domaini677 – 6826PeriplasmicCurated

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: GO_Central
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi377 – 3771F → A: Loss of ATPase activity. 1 Publication
Mutagenesisi377 – 3771F → Y: Slight decrease in ATPase activity. 1 Publication
Mutagenesisi384 – 3841S → A or T: Decrease in ATPase activity. 1 Publication
Mutagenesisi395 – 3951K → A: Strong decrease in ATPase activity. 1 Publication
Mutagenesisi399 – 3991D → A: Decrease in ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 682682Potassium-transporting ATPase ATP-binding subunitPRO_0000046115Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP03960.
PRIDEiP03960.

Expressioni

Inductioni

Transcriptionally regulated by the KdpD/KdpE two-component regulatory system.1 Publication

Interactioni

Subunit structurei

The system is composed of three essential subunits: KdpA, KdpB and KdpC (PubMed:2849541, PubMed:9858692). The complex also contains KdpF, a small non-essential subunit (PubMed:10608856). The KdpFABC complex exists as a dimer above concentrations of 30-50 nM, whereas the complex exists as a functional monomer at lower concentrations (PubMed:18298081).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
kdpCP039612EBI-1116956,EBI-6997216

Protein-protein interaction databases

BioGridi4263067. 15 interactions.
IntActiP03960. 8 interactions.
MINTiMINT-8188849.
STRINGi511145.b0697.

Structurei

Secondary structure

1
682
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi317 – 3248Combined sources
Helixi330 – 33910Combined sources
Helixi347 – 35913Combined sources
Helixi367 – 3704Combined sources
Beta strandi373 – 3786Combined sources
Turni379 – 3824Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi391 – 3977Combined sources
Helixi398 – 40811Combined sources
Helixi414 – 42512Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi438 – 44710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVJNMR-A316-451[»]
1U7QNMR-A316-451[»]
2A00NMR-A316-451[»]
2A29NMR-A316-451[»]
ProteinModelPortaliP03960.
SMRiP03960. Positions 38-600.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03960.

Family & Domainsi

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C8X. Bacteria.
COG2216. LUCA.
HOGENOMiHOG000244113.
InParanoidiP03960.
KOiK01547.
OMAiDWLVIQC.
OrthoDBiEOG6742RM.
PhylomeDBiP03960.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_00285. KdpB.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006391. P-type_ATPase_bsu_IA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01497. kdpB. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKQLALFE PTLVVQALKE AVKKLNPQAQ WRNPVMFIVW IGSLLTTCIS
60 70 80 90 100
IAMASGAMPG NALFSAAISG WLWITVLFAN FAEALAEGRS KAQANSLKGV
110 120 130 140 150
KKTAFARKLR EPKYGAAADK VPADQLRKGD IVLVEAGDII PCDGEVIEGG
160 170 180 190 200
ASVDESAITG ESAPVIRESG GDFASVTGGT RILSDWLVIE CSVNPGETFL
210 220 230 240 250
DRMIAMVEGA QRRKTPNEIA LTILLIALTI VFLLATATLW PFSAWGGNAV
260 270 280 290 300
SVTVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD
310 320 330 340 350
VDVLLLDKTG TITLGNRQAS EFIPAQGVDE KTLADAAQLA SLADETPEGR
360 370 380 390 400
SIVILAKQRF NLRERDVQSL HATFVPFTAQ SRMSGINIDN RMIRKGSVDA
410 420 430 440 450
IRRHVEANGG HFPTDVDQKV DQVARQGATP LVVVEGSRVL GVIALKDIVK
460 470 480 490 500
GGIKERFAQL RKMGIKTVMI TGDNRLTAAA IAAEAGVDDF LAEATPEAKL
510 520 530 540 550
ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ AAKEAGNMVD
560 570 580 590 600
LDSNPTKLIE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI IPAAFAATYP
610 620 630 640 650
QLNALNIMCL HSPDSAILSA VIFNALIIVF LIPLALKGVS YKPLTASAML
660 670 680
RRNLWIYGLG GLLVPFIGIK VIDLLLTVCG LV
Length:682
Mass (Da):72,199
Last modified:November 1, 1997 - v3
Checksum:i4718AE78ECDA476C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1122EP → DA in AAB96336 (PubMed:6146979).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02670 Genomic DNA. Translation: AAB96336.1.
U00096 Genomic DNA. Translation: AAC73791.1.
AP009048 Genomic DNA. Translation: BAA35354.1.
PIRiH64804. PWECBK.
RefSeqiNP_415225.1. NC_000913.3.
WP_000087939.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73791; AAC73791; b0697.
BAA35354; BAA35354; BAA35354.
GeneIDi947450.
KEGGiecj:JW0685.
eco:b0697.
PATRICi32116589. VBIEscCol129921_0727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02670 Genomic DNA. Translation: AAB96336.1.
U00096 Genomic DNA. Translation: AAC73791.1.
AP009048 Genomic DNA. Translation: BAA35354.1.
PIRiH64804. PWECBK.
RefSeqiNP_415225.1. NC_000913.3.
WP_000087939.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVJNMR-A316-451[»]
1U7QNMR-A316-451[»]
2A00NMR-A316-451[»]
2A29NMR-A316-451[»]
ProteinModelPortaliP03960.
SMRiP03960. Positions 38-600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263067. 15 interactions.
IntActiP03960. 8 interactions.
MINTiMINT-8188849.
STRINGi511145.b0697.

Protein family/group databases

TCDBi3.A.3.7.1. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiP03960.
PRIDEiP03960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73791; AAC73791; b0697.
BAA35354; BAA35354; BAA35354.
GeneIDi947450.
KEGGiecj:JW0685.
eco:b0697.
PATRICi32116589. VBIEscCol129921_0727.

Organism-specific databases

EchoBASEiEB0509.
EcoGeneiEG10514. kdpB.

Phylogenomic databases

eggNOGiENOG4105C8X. Bacteria.
COG2216. LUCA.
HOGENOMiHOG000244113.
InParanoidiP03960.
KOiK01547.
OMAiDWLVIQC.
OrthoDBiEOG6742RM.
PhylomeDBiP03960.

Enzyme and pathway databases

BioCyciEcoCyc:KDPB-MONOMER.
ECOL316407:JW0685-MONOMER.
MetaCyc:KDPB-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP03960.
PROiP03960.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_00285. KdpB.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006391. P-type_ATPase_bsu_IA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01497. kdpB. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum."
    Hesse J.E., Wieczorek L., Altendorf K., Reicin A.S., Dorus E., Epstein W.
    Proc. Natl. Acad. Sci. U.S.A. 81:4746-4750(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Epstein W.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 274-275 AND 456.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "The K+-translocating Kdp-ATPase from Escherichia coli. Purification, enzymatic properties and production of complex- and subunit-specific antisera."
    Siebers A., Altendorf K.
    Eur. J. Biochem. 178:131-140(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POTASSIUM TRANSPORT, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "The products of the kdpDE operon are required for expression of the Kdp ATPase of Escherichia coli."
    Polarek J.W., Williams G., Epstein W.
    J. Bacteriol. 174:2145-2151(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12.
  8. "ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli."
    Kollmann R., Altendorf K.
    Biochim. Biophys. Acta 1143:62-66(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POTASSIUM TRANSPORT.
    Strain: K12.
  9. "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli."
    Gassel M., Siebers A., Epstein W., Altendorf K.
    Biochim. Biophys. Acta 1415:77-84(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: K12.
  10. "The KdpF subunit is part of the K(+)-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro."
    Gassel M., Mollenkamp T., Puppe W., Altendorf K.
    J. Biol. Chem. 274:37901-37907(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: K12.
  11. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  12. "K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer."
    Heitkamp T., Kalinowski R., Boettcher B., Boersch M., Altendorf K., Greie J.C.
    Biochemistry 47:3564-3575(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  13. "Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase."
    Damnjanovic B., Weber A., Potschies M., Greie J.C., Apell H.J.
    Biochemistry 52:5563-5576(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes."
    Haupt M., Bramkamp M., Coles M., Altendorf K., Kessler H.
    J. Mol. Biol. 342:1547-1558(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 316-451.
  15. "The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode."
    Haupt M., Bramkamp M., Heller M., Coles M., Deckers-Hebestreit G., Herkenhoff-Hesselmann B., Altendorf K., Kessler H.
    J. Biol. Chem. 281:9641-9649(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 316-451 IN COMPLEX WITH ATP ANALOG, FUNCTION AS AN ATPASE, ATP-BINDING, MUTAGENESIS OF PHE-377; SER-384; LYS-395 AND ASP-399.

Entry informationi

Entry nameiKDPB_ECOLI
AccessioniPrimary (citable) accession number: P03960
Secondary accession number(s): P78053, P78145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.