Potassium-transporting ATPase B chain - Escherichia coli (strain K12)

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P03960 (ATKB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Potassium-transporting ATPase B chain
EC=3.6.3.12

Alternative name(s):
ATP phosphohydrolase [potassium-transporting] B chain
Potassium-binding and translocating subunit B
Potassium-translocating ATPase B chain

Gene names

Name:	kdpB
Ordered Locus Names:	b0697, JW0685

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	682 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the components of the high-affinity ATP-driven potassium transport (or KDP) system, which catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions. HAMAP MF_00285
Catalytic activity	ATP + H₂O + K⁺(Out) = ADP + phosphate + K⁺(In). HAMAP MF_00285
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.6.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from direct assay. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium-transporting ATPase activity Inferred from mutant phenotype. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 682

682

Potassium-transporting ATPase B chain HAMAP MF_00285

PRO_0000046115

Regions

Topological domain

1 – 35

Cytoplasmic Potential

Transmembrane

36 – 58

Helical; Potential

Topological domain

59 – 62

Periplasmic Potential

Transmembrane

63 – 85

Helical; Potential

Topological domain

86 – 219

134

Cytoplasmic Potential

Transmembrane

220 – 242

Helical; Potential

Topological domain

243 – 251

Periplasmic Potential

Transmembrane

252 – 274

Helical; Potential

Topological domain

275 – 577

303

Cytoplasmic Potential

Transmembrane

578 – 600

Helical; Potential

Topological domain

601 – 614

Periplasmic Potential

Transmembrane

615 – 634

Helical; Potential

Topological domain

635 – 653

Cytoplasmic Potential

Transmembrane

654 – 676

Helical; Potential

Topological domain

677 – 682

Periplasmic Potential

Sites

Active site

307

4-aspartylphosphate intermediate By similarity

Metal binding

518

Magnesium By similarity

Metal binding

522

Magnesium By similarity

Experimental info

Sequence conflict

111 – 112

EP → DA in AAB96336. Ref.1

Secondary structure

682

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03960 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 4718AE78ECDA476C
Show »

FASTA

682

72,199

        10         20         30         40         50         60 
MSRKQLALFE PTLVVQALKE AVKKLNPQAQ WRNPVMFIVW IGSLLTTCIS IAMASGAMPG 

        70         80         90        100        110        120 
NALFSAAISG WLWITVLFAN FAEALAEGRS KAQANSLKGV KKTAFARKLR EPKYGAAADK 

       130        140        150        160        170        180 
VPADQLRKGD IVLVEAGDII PCDGEVIEGG ASVDESAITG ESAPVIRESG GDFASVTGGT 

       190        200        210        220        230        240 
RILSDWLVIE CSVNPGETFL DRMIAMVEGA QRRKTPNEIA LTILLIALTI VFLLATATLW 

       250        260        270        280        290        300 
PFSAWGGNAV SVTVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD 

       310        320        330        340        350        360 
VDVLLLDKTG TITLGNRQAS EFIPAQGVDE KTLADAAQLA SLADETPEGR SIVILAKQRF 

       370        380        390        400        410        420 
NLRERDVQSL HATFVPFTAQ SRMSGINIDN RMIRKGSVDA IRRHVEANGG HFPTDVDQKV 

       430        440        450        460        470        480 
DQVARQGATP LVVVEGSRVL GVIALKDIVK GGIKERFAQL RKMGIKTVMI TGDNRLTAAA 

       490        500        510        520        530        540 
IAAEAGVDDF LAEATPEAKL ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ 

       550        560        570        580        590        600 
AAKEAGNMVD LDSNPTKLIE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI IPAAFAATYP 

       610        620        630        640        650        660 
QLNALNIMCL HSPDSAILSA VIFNALIIVF LIPLALKGVS YKPLTASAML RRNLWIYGLG 

       670        680 
GLLVPFIGIK VIDLLLTVCG LV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6146979] [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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"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: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02670 Genomic DNA. Translation: AAB96336.1.
U00096 Genomic DNA. Translation: AAC73791.1.
AP009048 Genomic DNA. Translation: BAA35354.1.

PIR

PWECBK. H64804.

RefSeq

NP_415225.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P03960.

SMR

P03960. Positions 62-628.

ModBase

Search...

Protein-protein interaction databases

IntAct

P03960. 7 interactions.

Protein family/group databases

TCDB

3.A.3.7.1. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003287; EBESCP00000003287; EBESCG00000002696.
EBESCT00000014601; EBESCP00000013892; EBESCG00000013662.

GeneID

947450.

GenomeReviews

Gene locus JW0685 in contig AP009048_GR.
Gene locus b0697 in contig U00096_GR.

KEGG

ecj:JW0685.
eco:b0697.

PATRIC

32116589. VBIEscCol129921_0727.

Organism-specific databases

EchoBASE

EB0509.

EcoGene

EG10514. kdpB.

Phylogenomic databases

eggNOG

COG2216.

GeneTree

EBGT00050000009754.

HOGENOM

HBG289193.

OMA

MHLATPA.

PhylomeDB

P03960.

ProtClustDB

PRK01122.

Enzyme and pathway databases

BioCyc

EcoCyc:KDPB-MONOMER.

Gene expression databases

Genevestigator

P03960.

Family and domain databases

HAMAP

MF_00285. KdpB.
[Tree]

InterPro

IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR006391. K-transp_ATPase_bsu.
[Graphical view]

Gene3D

G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.

K01547.

PANTHER

PTHR24093:SF27. PTHR24093:SF27. 1 hit.

Pfam

PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01494. ATPase_P-type. 2 hits.
TIGR01497. KdpB. 1 hit.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATKB_ECOLI

Accession

Primary (citable) accession number: P03960
Secondary accession number(s): P78053, P78145

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents