UniProtKB - P03960 (KDPB_ECOLI)

BLAST

>sp|P03960|KDPB_ECOLI Potassium-transporting ATPase ATP-binding subunit OS=Escherichia coli (strain K12) OX=83333 GN=kdpB PE=1 SV=3
MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPG
NALFSAAISGWLWITVLFANFAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADK
VPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGT
RILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLW
PFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGD
VDVLLLDKTGTITLGNRQASEFIPAQGVDEKTLADAAQLASLADETPEGRSIVILAKQRF
NLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDAIRRHVEANGGHFPTDVDQKV
DQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAA
IAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQ
AAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYP
QLNALNIMCLHSPDSAILSAVIFNALIIVFLIPLALKGVSYKPLTASAMLRRNLWIYGLG
GLLVPFIGIKVIDLLLTVCGLV

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History
Entry version 176 (07 Nov 2018)
Sequence version 3 (01 Nov 1997)
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Protein

Potassium-transporting ATPase ATP-binding subunit

Gene

kdpB

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -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

Activity regulationⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	307	4-aspartylphosphate intermediateUniRule annotation	1
Binding siteⁱ	344	ATPUniRule annotationCombined sources1 Publication	1
Binding siteⁱ	348	ATPUniRule annotationCombined sources1 Publication	1
Binding siteⁱ	395	ATPUniRule annotationCombined sources1 Publication	1
Metal bindingⁱ	518	MagnesiumUniRule annotation	1
Metal bindingⁱ	522	MagnesiumUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	377 – 384	ATPUniRule annotationCombined sources1 Publication		8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-UniRule
magnesium ion binding Source: UniProtKB-UniRule
potassium-transporting ATPase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 8499455
- 9789555

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

ATP hydrolysis coupled cation transmembrane transport
Source: EcoCyc
Inferred from direct assayⁱ
- 8499455
potassium ion transmembrane transport
Source: EcoCyc
Inferred from direct assayⁱ
- 8499455
- 9789555
potassium ion transport
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 17994765

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Ion transport, Potassium transport, Transport
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCycⁱ	EcoCyc:KDPB-MONOMER MetaCyc:KDPB-MONOMER

BioCycⁱ

EcoCyc:KDPB-MONOMER
MetaCyc:KDPB-MONOMER

Protein family/group databases

TCDBⁱ	3.A.3.7.1 the p-type atpase (p-atpase) superfamily

TCDBⁱ

3.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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10514 kdpB

EcoGeneⁱ

EG10514 kdpB

Subcellular locationⁱ

Cell inner membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00285
2 Publications
Manual assertion based on experiment inⁱ
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.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.
; Multi-pass membrane protein
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00285
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 33	CytoplasmicCuratedAdd BLAST	33
Transmembraneⁱ	34 – 54	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	55 – 61	PeriplasmicCurated	7
Transmembraneⁱ	62 – 82	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	83 – 218	CytoplasmicCuratedAdd BLAST	136
Transmembraneⁱ	219 – 239	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	240 – 253	PeriplasmicCuratedAdd BLAST	14
Transmembraneⁱ	254 – 274	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	275 – 587	CytoplasmicCuratedAdd BLAST	313
Transmembraneⁱ	588 – 608	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	609 – 615	PeriplasmicCurated	7
Transmembraneⁱ	616 – 636	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	637 – 655	CytoplasmicCuratedAdd BLAST	19
Transmembraneⁱ	656 – 676	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	677 – 682	PeriplasmicCurated	6

GO - Cellular componentⁱ

integral component of membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 17994765
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 28636601
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15919996
- 356049
potassium ion-transporting ATPase complex
Source: EcoCyc
Inferred from direct assayⁱ
- 28636601

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	377	F → A: Loss of ATPase activity. 1 Publication	1
Mutagenesisⁱ	377	F → Y: Slight decrease in ATPase activity. 1 Publication	1
Mutagenesisⁱ	384	S → A or T: Decrease in ATPase activity. 1 Publication	1
Mutagenesisⁱ	395	K → A: Strong decrease in ATPase activity. 1 Publication	1
Mutagenesisⁱ	399	D → A: Decrease in ATPase activity. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

DrugBankⁱ

DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000046115	1 – 682	Potassium-transporting ATPase ATP-binding subunitAdd BLAST		682

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

PaxDbⁱ	P03960
PRIDEⁱ	P03960

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

With	Entry	#Exp.	IntAct	Notes
kdpC	P03961	2	EBI-1116956,EBI-6997216

With

Entry

#Exp.

IntAct

Notes

kdpC

P03961

EBI-1116956,EBI-6997216

Protein-protein interaction databases

BioGridⁱ	4263067, 21 interactors
ComplexPortalⁱ	CPX-3564 KdpFABC potassium import complex
IntActⁱ	P03960, 9 interactors
Molecular INTeraction database More...MINTⁱ	P03960
STRINGⁱ	316385.ECDH10B_0763

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	12 – 23	Combined sources	12
Helixⁱ	34 – 56	Combined sources	23
Helixⁱ	63 – 102	Combined sources	40
Beta strandⁱ	107 – 113	Combined sources	7
Beta strandⁱ	118 – 120	Combined sources	3
Helixⁱ	123 – 125	Combined sources	3
Beta strandⁱ	131 – 134	Combined sources	4
Beta strandⁱ	144 – 154	Combined sources	11
Helixⁱ	156 – 159	Combined sources	4
Beta strandⁱ	164 – 171	Combined sources	8
Beta strandⁱ	187 – 190	Combined sources	4
Helixⁱ	199 – 207	Combined sources	9
Beta strandⁱ	208 – 211	Combined sources	4
Helixⁱ	216 – 237	Combined sources	22
Helixⁱ	239 – 246	Combined sources	8
Helixⁱ	252 – 262	Combined sources	11
Helixⁱ	265 – 268	Combined sources	4
Helixⁱ	271 – 284	Combined sources	14
Helixⁱ	292 – 299	Combined sources	8
Beta strandⁱ	302 – 307	Combined sources	6
Beta strandⁱ	311 – 315	Combined sources	5
Beta strandⁱ	317 – 323	Combined sources	7
Helixⁱ	330 – 341	Combined sources	12
Helixⁱ	347 – 360	Combined sources	14
Helixⁱ	367 – 370	Combined sources	4
Beta strandⁱ	374 – 378	Combined sources	5
Turnⁱ	379 – 382	Combined sources	4
Beta strandⁱ	383 – 386	Combined sources	4
Beta strandⁱ	389 – 391	Combined sources	3
Beta strandⁱ	393 – 396	Combined sources	4
Helixⁱ	398 – 405	Combined sources	8
Helixⁱ	406 – 408	Combined sources	3
Helixⁱ	414 – 426	Combined sources	13
Beta strandⁱ	429 – 435	Combined sources	7
Beta strandⁱ	438 – 447	Combined sources	10
Helixⁱ	453 – 462	Combined sources	10
Beta strandⁱ	466 – 470	Combined sources	5
Helixⁱ	477 – 485	Combined sources	9
Beta strandⁱ	488 – 491	Combined sources	4
Helixⁱ	496 – 507	Combined sources	12
Turnⁱ	508 – 510	Combined sources	3
Beta strandⁱ	513 – 518	Combined sources	6
Turnⁱ	519 – 522	Combined sources	4
Helixⁱ	523 – 528	Combined sources	6
Beta strandⁱ	529 – 536	Combined sources	8
Helixⁱ	539 – 545	Combined sources	7
Beta strandⁱ	548 – 552	Combined sources	5
Helixⁱ	557 – 581	Combined sources	25
Helixⁱ	583 – 594	Combined sources	12
Turnⁱ	595 – 598	Combined sources	4
Helixⁱ	600 – 605	Combined sources	6
Helixⁱ	613 – 637	Combined sources	25
Helixⁱ	646 – 679	Combined sources	34

Show more details

3D structure databases

ProteinModelPortalⁱ	P03960
SMRⁱ	P03960
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P03960

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

eggNOGⁱ	ENOG4105C8X Bacteria COG2216 LUCA
HOGENOMⁱ	HOG000244113
InParanoidⁱ	P03960
KEGG Orthology (KO) More...KOⁱ	K01547
PhylomeDBⁱ	P03960

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02078 P-type_ATPase_K, 1 hit
Gene3Dⁱ	3.40.1110.10, 1 hit 3.40.50.1000, 1 hit
HAMAPⁱ	MF_00285 KdpB, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR43743 PTHR43743, 1 hit
SUPFAMⁱ	SSF56784 SSF56784, 1 hit SSF81653 SSF81653, 1 hit SSF81660 SSF81660, 1 hit SSF81665 SSF81665, 1 hit
TIGRFAMsⁱ	TIGR01494 ATPase_P-type, 2 hits TIGR01497 kdpB, 1 hit
PROSITEⁱ	View protein in PROSITE PS00154 ATPASE_E1_E2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P03960-1 [UniParc]FASTA Add 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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	111 – 112	EP → DA in AAB96336 (PubMed:6146979).Curated		2

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
PIRⁱ	H64804 PWECBK
NCBI Reference Sequences More...RefSeqⁱ	NP_415225.1, NC_000913.3 WP_000087939.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73791; AAC73791; b0697 BAA35354; BAA35354; BAA35354
GeneIDⁱ	947450
KEGGⁱ	ecj:JW0685 eco:b0697
PATRICⁱ	fig\|1411691.4.peg.1578

Protein	Similar proteins		Species	Score	Length	Source
P03960	Potassium-transporting ATPase ATP-binding subunit		ECOBW		682	UniRef100_C4ZWH3
Potassium-transporting ATPase ATP-binding subunit		ECODH		682
Potassium-transporting ATPase subunit B		Shigella sp.		682
Potassium-transporting ATPase ATP-binding subunit		ECOLX		682
Potassium-transporting ATPase ATP-binding subunit		SHIDY		682
+21

Protein	Similar proteins		Species	Score	Length	Source
P03960	Potassium-transporting ATPase ATP-binding subunit		SALTY		682	UniRef90_Q8ZQW2
Potassium-transporting ATPase ATP-binding subunit		SALG2		685
Potassium-transporting ATPase ATP-binding subunit		SALEP		682
Potassium-transporting ATPase ATP-binding subunit		SALHS		682
Potassium-transporting ATPase ATP-binding subunit		SALDC		682
+1997

Protein	Similar proteins		Species	Score	Length	Source
P03960	Potassium-transporting ATPase ATP-binding subunit		CLOAB		685	UniRef50_O32328
Potassium-transporting ATPase ATP-binding subunit		LISMH		681
Potassium-transporting ATPase ATP-binding subunit		LISW6		681
Potassium-transporting ATPase ATP-binding subunit		LISMO		681
Potassium-transporting ATPase ATP-binding subunit 1		LISIN		681
+14242

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
PIRⁱ	H64804 PWECBK
RefSeqⁱ	NP_415225.1, NC_000913.3 WP_000087939.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1SVJ	NMR	-	A	316-451	[»]
	1U7Q	NMR	-	A	316-451	[»]
	2A00	NMR	-	A	316-451	[»]
	2A29	NMR	-	A	316-451	[»]
	5MRW	X-ray	2.90	B/F/J	9-682	[»]
ProteinModelPortalⁱ	P03960
SMRⁱ	P03960
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263067, 21 interactors
ComplexPortalⁱ	CPX-3564 KdpFABC potassium import complex
IntActⁱ	P03960, 9 interactors
MINTⁱ	P03960
STRINGⁱ	316385.ECDH10B_0763

Chemistry databases

DrugBankⁱ	DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

DrugBankⁱ

DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

Protein family/group databases

TCDBⁱ	3.A.3.7.1 the p-type atpase (p-atpase) superfamily

TCDBⁱ

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

Proteomic databases

PaxDbⁱ	P03960
PRIDEⁱ	P03960

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73791; AAC73791; b0697 BAA35354; BAA35354; BAA35354
GeneIDⁱ	947450
KEGGⁱ	ecj:JW0685 eco:b0697
PATRICⁱ	fig\|1411691.4.peg.1578

Organism-specific databases

EchoBASEⁱ	EB0509
EcoGeneⁱ	EG10514 kdpB

Phylogenomic databases

eggNOGⁱ	ENOG4105C8X Bacteria COG2216 LUCA
HOGENOMⁱ	HOG000244113
InParanoidⁱ	P03960
KOⁱ	K01547
PhylomeDBⁱ	P03960

Enzyme and pathway databases

BioCycⁱ	EcoCyc:KDPB-MONOMER MetaCyc:KDPB-MONOMER

BioCycⁱ

EcoCyc:KDPB-MONOMER
MetaCyc:KDPB-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P03960
Protein Ontology More...PROⁱ	PR:P03960

Family and domain databases

CDDⁱ	cd02078 P-type_ATPase_K, 1 hit
Gene3Dⁱ	3.40.1110.10, 1 hit 3.40.50.1000, 1 hit
HAMAPⁱ	MF_00285 KdpB, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR43743 PTHR43743, 1 hit
SUPFAMⁱ	SSF56784 SSF56784, 1 hit SSF81653 SSF81653, 1 hit SSF81660 SSF81660, 1 hit SSF81665 SSF81665, 1 hit
TIGRFAMsⁱ	TIGR01494 ATPase_P-type, 2 hits TIGR01497 kdpB, 1 hit
PROSITEⁱ	View protein in PROSITE PS00154 ATPASE_E1_E2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KDPB_ECOLI
Accessionⁱ	P03960Primary (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 7, 2018
	This is version 176 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P03960 (KDPB_ECOLI)

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Potassium-transporting ATPase ATP-binding subunit

kdpB

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Keywords - PTMi

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ