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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-KW
  • metal ion binding Source: UniProtKB-KW
  • potassium-transporting ATPase activity Source: EcoliWiki

GO - Biological processi

  • potassium ion transport Source: EcoliWiki

Keywordsi

Molecular functionHydrolase
Biological processIon transport, Potassium transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:KDPB-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
  • plasma membrane Source: EcoCyc

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

Chemistry databases

DrugBankiDB04395. Phosphoaminophosphonic Acid-Adenylate Ester.

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.
STRINGi316385.ECDH10B_0763.

Structurei

Secondary structure

1682
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 23Combined sources12
Helixi34 – 56Combined sources23
Helixi63 – 102Combined sources40
Beta strandi107 – 113Combined sources7
Beta strandi118 – 120Combined sources3
Helixi123 – 125Combined sources3
Beta strandi131 – 134Combined sources4
Beta strandi144 – 154Combined sources11
Helixi156 – 159Combined sources4
Beta strandi164 – 171Combined sources8
Beta strandi187 – 190Combined sources4
Helixi199 – 207Combined sources9
Beta strandi208 – 211Combined sources4
Helixi216 – 237Combined sources22
Helixi239 – 246Combined sources8
Helixi252 – 262Combined sources11
Helixi265 – 268Combined sources4
Helixi271 – 284Combined sources14
Helixi292 – 299Combined sources8
Beta strandi302 – 307Combined sources6
Beta strandi311 – 315Combined sources5
Beta strandi317 – 323Combined sources7
Helixi330 – 341Combined sources12
Helixi347 – 360Combined sources14
Helixi367 – 370Combined sources4
Beta strandi374 – 378Combined sources5
Turni379 – 382Combined sources4
Beta strandi383 – 386Combined sources4
Beta strandi389 – 391Combined sources3
Beta strandi393 – 396Combined sources4
Helixi398 – 405Combined sources8
Helixi406 – 408Combined sources3
Helixi414 – 426Combined sources13
Beta strandi429 – 435Combined sources7
Beta strandi438 – 447Combined sources10
Helixi453 – 462Combined sources10
Beta strandi466 – 470Combined sources5
Helixi477 – 485Combined sources9
Beta strandi488 – 491Combined sources4
Helixi496 – 507Combined sources12
Turni508 – 510Combined sources3
Beta strandi513 – 518Combined sources6
Turni519 – 522Combined sources4
Helixi523 – 528Combined sources6
Beta strandi529 – 536Combined sources8
Helixi539 – 545Combined sources7
Beta strandi548 – 552Combined sources5
Helixi557 – 581Combined sources25
Helixi583 – 594Combined sources12
Turni595 – 598Combined sources4
Helixi600 – 605Combined sources6
Helixi613 – 637Combined sources25
Helixi646 – 679Combined sources34

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[»]
5MRWX-ray2.90B/F/J9-682[»]
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.
PhylomeDBiP03960.

Family and domain databases

CDDicd02078. P-type_ATPase_K. 1 hit.
Gene3Di3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_00285. KdpB. 1 hit.
InterProiView protein in InterPro
IPR023299. ATPase_P-typ_cyto_dom_N.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom_sf.
IPR008250. ATPase_P-typ_transduc_dom_A_sf.
IPR036412. HAD-like_sf.
IPR023214. HAD_sf.
IPR006391. P-type_ATPase_bsu_IA.
IPR001757. P_typ_ATPase.
PANTHERiPTHR43743. PTHR43743. 1 hit.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81653. SSF81653. 1 hit.
SSF81660. SSF81660. 1 hit.
SSF81665. SSF81665. 3 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01497. kdpB. 1 hit.
PROSITEiView protein in PROSITE
PS00154. ATPASE_E1_E2. 1 hit.

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.
PATRICifig|1411691.4.peg.1578.

Similar proteinsi

Entry informationi

Entry nameiKDPB_ECOLI
AccessioniPrimary (citable) accession number: P03960
Secondary accession number(s): P78053, P78145
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 170 of the entry and version 3 of the sequence. See 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