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Protein

Ktr system potassium uptake protein A

Gene

ktrA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161NAD2 Publications
Binding sitei109 – 1091NAD2 Publications
Binding sitei125 – 1251NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 383NAD2 Publications
Nucleotide bindingi56 – 572NAD2 Publications
Nucleotide bindingi78 – 803NAD2 Publications
Nucleotide bindingi103 – 1053NAD2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

NAD, Potassium

Enzyme and pathway databases

BioCyciBSUB:BSU31090-MONOMER.

Protein family/group databases

TCDBi2.A.38.4.3. the k(+) transporter (trk) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ktr system potassium uptake protein A
Short name:
K(+)-uptake protein KtrA
Gene namesi
Name:ktrA
Synonyms:yuaA
Ordered Locus Names:BSU31090
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Impaired potassium uptake.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Ktr system potassium uptake protein APRO_0000360619Add
BLAST

Proteomic databases

PaxDbiO32080.

Interactioni

Subunit structurei

Homodimer, tetramer (dimer of homodimer) and octamer (tetramer of homodimer). Part of the KtrAB complex formed by an octameric catalytic ring of KtrA and a membrane associated dimer of KtrB forming a potassium channel.2 Publications

Protein-protein interaction databases

DIPiDIP-60209N.
STRINGi224308.Bsubs1_010100016906.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi16 – 2712Combined sources
Beta strandi33 – 375Combined sources
Helixi39 – 435Combined sources
Turni44 – 485Combined sources
Beta strandi50 – 545Combined sources
Helixi60 – 645Combined sources
Turni65 – 673Combined sources
Helixi68 – 703Combined sources
Beta strandi72 – 765Combined sources
Helixi82 – 9413Combined sources
Beta strandi98 – 1036Combined sources
Helixi107 – 11610Combined sources
Beta strandi119 – 1224Combined sources
Helixi124 – 14017Combined sources
Turni141 – 1433Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi153 – 1564Combined sources
Helixi160 – 1623Combined sources
Turni167 – 1693Combined sources
Helixi172 – 1754Combined sources
Beta strandi179 – 1857Combined sources
Beta strandi188 – 1925Combined sources
Beta strandi205 – 2095Combined sources
Helixi211 – 22111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LSUX-ray2.85A/B1-143[»]
2HMSX-ray2.70A/B/C/D1-144[»]
2HMTX-ray2.20A/B1-144[»]
2HMUX-ray2.25A/B1-144[»]
2HMVX-ray2.20A/B1-144[»]
2HMWX-ray3.00A/B1-144[»]
4J7CX-ray3.50A/B/C/D/E/F/G/H1-222[»]
4J90X-ray3.24A/B1-222[»]
4J91X-ray2.93A/B/C/D1-222[»]
5BUTX-ray5.97A/C/E/G1-212[»]
ProteinModelPortaliO32080.
SMRiO32080. Positions 6-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32080.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 130123RCK N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini139 – 22284RCK C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the KtrA potassium transport family.Curated
Contains 1 RCK C-terminal domain.PROSITE-ProRule annotation
Contains 1 RCK N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0569. LUCA.
HOGENOMiHOG000279860.
InParanoidiO32080.
KOiK03499.
OMAiLNVRAKY.
OrthoDBiEOG6HQSSJ.
PhylomeDBiO32080.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRIKNKQFA VIGLGRFGGS ICKELHRMGH EVLAVDINEE KVNAYASYAT
60 70 80 90 100
HAVIANATEE NELLSLGIRN FEYVIVAIGA NIQASTLTTL LLKELDIPNI
110 120 130 140 150
WVKAQNYYHH KVLEKIGADR IIHPEKDMGV KIAQSLSDEN VLNYIDLSDE
160 170 180 190 200
YSIVELLATR KLDSKSIIDL NVRAKYGCTI LAIKHHGDIC LSPAPEDIIR
210 220
EQDCLVIMGH KKDIKRFENE GM
Length:222
Mass (Da):24,882
Last modified:January 1, 1998 - v1
Checksum:i24E32EDB155E806F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15087.1.
PIRiC70005.
RefSeqiNP_390987.1. NC_000964.3.
WP_003243377.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15087; CAB15087; BSU31090.
GeneIDi937145.
KEGGibsu:BSU31090.
PATRICi18978172. VBIBacSub10457_3250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15087.1.
PIRiC70005.
RefSeqiNP_390987.1. NC_000964.3.
WP_003243377.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LSUX-ray2.85A/B1-143[»]
2HMSX-ray2.70A/B/C/D1-144[»]
2HMTX-ray2.20A/B1-144[»]
2HMUX-ray2.25A/B1-144[»]
2HMVX-ray2.20A/B1-144[»]
2HMWX-ray3.00A/B1-144[»]
4J7CX-ray3.50A/B/C/D/E/F/G/H1-222[»]
4J90X-ray3.24A/B1-222[»]
4J91X-ray2.93A/B/C/D1-222[»]
5BUTX-ray5.97A/C/E/G1-212[»]
ProteinModelPortaliO32080.
SMRiO32080. Positions 6-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60209N.
STRINGi224308.Bsubs1_010100016906.

Protein family/group databases

TCDBi2.A.38.4.3. the k(+) transporter (trk) family.

Proteomic databases

PaxDbiO32080.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15087; CAB15087; BSU31090.
GeneIDi937145.
KEGGibsu:BSU31090.
PATRICi18978172. VBIBacSub10457_3250.

Phylogenomic databases

eggNOGiCOG0569. LUCA.
HOGENOMiHOG000279860.
InParanoidiO32080.
KOiK03499.
OMAiLNVRAKY.
OrthoDBiEOG6HQSSJ.
PhylomeDBiO32080.

Enzyme and pathway databases

BioCyciBSUB:BSU31090-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32080.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity."
    Holtmann G., Bakker E.P., Uozumi N., Bremer E.
    J. Bacteriol. 185:1289-1298(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  3. "A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch."
    Roosild T.P., Miller S., Booth I.R., Choe S.
    Cell 109:781-791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-142 IN COMPLEX WITH NAD, SUBUNIT.
  4. "The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring."
    Albright R.A., Ibar J.-L.V., Kim C.U., Gruner S.M., Morais-Cabral J.H.
    Cell 126:1147-1159(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-144 IN COMPLEX WITH NAD, INTERACTION WITH KTRB, SUBUNIT.

Entry informationi

Entry nameiKTRA_BACSU
AccessioniPrimary (citable) accession number: O32080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: March 16, 2016
This is version 107 of the entry and version 1 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.