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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)DescriptionActionsGraphical viewLength
Active sitei3074-aspartylphosphate intermediateUniRule annotation1
Binding sitei344ATPUniRule annotationCombined sources1 Publication1
Binding sitei348ATPUniRule annotationCombined sources1 Publication1
Binding sitei395ATPUniRule annotationCombined sources1 Publication1
Metal bindingi518MagnesiumUniRule annotation1
Metal bindingi522MagnesiumUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi377 – 384ATPUniRule annotationCombined sources1 Publication8

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10514. kdpB.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 33CytoplasmicCuratedAdd BLAST33
Transmembranei34 – 54HelicalUniRule annotationAdd BLAST21
Topological domaini55 – 61PeriplasmicCurated7
Transmembranei62 – 82HelicalUniRule annotationAdd BLAST21
Topological domaini83 – 218CytoplasmicCuratedAdd BLAST136
Transmembranei219 – 239HelicalUniRule annotationAdd BLAST21
Topological domaini240 – 253PeriplasmicCuratedAdd BLAST14
Transmembranei254 – 274HelicalUniRule annotationAdd BLAST21
Topological domaini275 – 587CytoplasmicCuratedAdd BLAST313
Transmembranei588 – 608HelicalUniRule annotationAdd BLAST21
Topological domaini609 – 615PeriplasmicCurated7
Transmembranei616 – 636HelicalUniRule annotationAdd BLAST21
Topological domaini637 – 655CytoplasmicCuratedAdd BLAST19
Transmembranei656 – 676HelicalUniRule annotationAdd BLAST21
Topological domaini677 – 682PeriplasmicCurated6

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)DescriptionActionsGraphical viewLength
Mutagenesisi377F → A: Loss of ATPase activity. 1 Publication1
Mutagenesisi377F → Y: Slight decrease in ATPase activity. 1 Publication1
Mutagenesisi384S → A or T: Decrease in ATPase activity. 1 Publication1
Mutagenesisi395K → A: Strong decrease in ATPase activity. 1 Publication1
Mutagenesisi399D → A: Decrease in ATPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000461151 – 682Potassium-transporting ATPase ATP-binding subunitAdd BLAST682

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 interactors.
IntActiP03960. 8 interactors.
MINTiMINT-8188849.
STRINGi511145.b0697.

Structurei

Secondary structure

1682
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi317 – 324Combined sources8
Helixi330 – 339Combined sources10
Helixi347 – 359Combined sources13
Helixi367 – 370Combined sources4
Beta strandi373 – 378Combined sources6
Turni379 – 382Combined sources4
Beta strandi383 – 388Combined sources6
Beta strandi391 – 397Combined sources7
Helixi398 – 408Combined sources11
Helixi414 – 425Combined sources12
Beta strandi429 – 435Combined sources7
Beta strandi438 – 447Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SVJNMR-A316-451[»]
1U7QNMR-A316-451[»]
2A00NMR-A316-451[»]
2A29NMR-A316-451[»]
ProteinModelPortaliP03960.
SMRiP03960.
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.
OMAiMFTVEIG.
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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti111 – 112EP → DA in AAB96336 (PubMed:6146979).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SVJNMR-A316-451[»]
1U7QNMR-A316-451[»]
2A00NMR-A316-451[»]
2A29NMR-A316-451[»]
ProteinModelPortaliP03960.
SMRiP03960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263067. 15 interactors.
IntActiP03960. 8 interactors.
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.
OMAiMFTVEIG.
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. 1 hit.
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...

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: November 2, 2016
This is version 162 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.