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Database: UniProt
Entry: O32081
LinkDB: O32081
Original site: O32081 
ID   KTRB_BACSU              Reviewed;         445 AA.
AC   O32081;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-JUN-2021, entry version 106.
DE   RecName: Full=Ktr system potassium uptake protein B;
DE            Short=K(+)-uptake protein KtrB;
GN   Name=ktrB; Synonyms=yubG; OrderedLocusNames=BSU31100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12562800; DOI=10.1128/jb.185.4.1289-1298.2003;
RA   Holtmann G., Bakker E.P., Uozumi N., Bremer E.;
RT   "KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role
RT   in adaptation to hypertonicity.";
RL   J. Bacteriol. 185:1289-1298(2003).
RN   [3]
RP   INTERACTION WITH KTRA, AND SUBUNIT.
RX   PubMed=16990138; DOI=10.1016/j.cell.2006.08.028;
RA   Albright R.A., Ibar J.-L.V., Kim C.U., Gruner S.M., Morais-Cabral J.H.;
RT   "The RCK domain of the KtrAB K+ transporter: multiple conformations of an
RT   octameric ring.";
RL   Cell 126:1147-1159(2006).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF 436-ARG--GLY-445, AND SUBUNIT.
RX   PubMed=17932047; DOI=10.1074/jbc.m704260200;
RA   Albright R.A., Joh K., Morais-Cabral J.H.;
RT   "Probing the structure of the dimeric KtrB membrane protein.";
RL   J. Biol. Chem. 282:35046-35055(2007).
CC   -!- FUNCTION: Integral membrane subunit of the KtrAB potassium uptake
CC       transporter. The 2 major potassium transporter complexes KtrAB and
CC       KtrCD confer resistance to both suddenly imposed and prolonged osmotic
CC       stress. {ECO:0000269|PubMed:12562800, ECO:0000269|PubMed:17932047}.
CC   -!- SUBUNIT: Homodimer. Part of the KtrAB complex formed by an octameric
CC       catalytic ring of KtrA and a membrane associated dimer of KtrB forming
CC       a potassium channel. {ECO:0000269|PubMed:16990138,
CC       ECO:0000269|PubMed:17932047}.
CC   -!- INTERACTION:
CC       O32081; O32080: ktrA; NbExp=2; IntAct=EBI-16045470, EBI-16045427;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Impaired potassium uptake.
CC       {ECO:0000269|PubMed:12562800}.
CC   -!- SIMILARITY: Belongs to the TrkH potassium transport family. Ktr (TC
CC       2.A.38.4) subfamily. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15088.1; -; Genomic_DNA.
DR   PIR; B70007; B70007.
DR   RefSeq; NP_390988.1; NC_000964.3.
DR   RefSeq; WP_003243582.1; NZ_JNCM01000033.1.
DR   PDB; 4J7C; X-ray; 3.50 A; I/J/K/L=1-445.
DR   PDB; 5BUT; X-ray; 5.97 A; I/J/K/L=1-445.
DR   PDBsum; 4J7C; -.
DR   PDBsum; 5BUT; -.
DR   SMR; O32081; -.
DR   DIP; DIP-60210N; -.
DR   IntAct; O32081; 1.
DR   STRING; 224308.BSU31100; -.
DR   TCDB; 2.A.38.4.3; the k(+) transporter (trk) family.
DR   PaxDb; O32081; -.
DR   EnsemblBacteria; CAB15088; CAB15088; BSU_31100.
DR   GeneID; 938835; -.
DR   KEGG; bsu:BSU31100; -.
DR   PATRIC; fig|224308.179.peg.3370; -.
DR   eggNOG; COG0168; Bacteria.
DR   InParanoid; O32081; -.
DR   OMA; WLAAFFQ; -.
DR   PhylomeDB; O32081; -.
DR   BioCyc; BSUB:BSU31100-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR   InterPro; IPR003445; Cat_transpt.
DR   InterPro; IPR004772; TrkH.
DR   Pfam; PF02386; TrkH; 1.
DR   TIGRFAMs; TIGR00933; 2a38; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Ion transport; Membrane; Potassium;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..445
FT                   /note="Ktr system potassium uptake protein B"
FT                   /id="PRO_0000360618"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         436..445
FT                   /note="Missing: Loss of homodimerization."
FT                   /evidence="ECO:0000269|PubMed:17932047"
FT   HELIX           16..36
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           47..58
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           74..89
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           91..101
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           108..117
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           126..145
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           161..173
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           192..206
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           226..250
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           254..258
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           264..274
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   TURN            275..279
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           291..302
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           316..330
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           345..372
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           377..388
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           403..418
FT                   /evidence="ECO:0007829|PDB:4J7C"
FT   HELIX           420..424
FT                   /evidence="ECO:0007829|PDB:4J7C"
SQ   SEQUENCE   445 AA;  48437 MW;  94AFD060587FD117 CRC64;
     MTLQKDKVIK WVRFTPPQVL AIGFFLTIII GAVLLMLPIS TTKPLSWIDA LFTAASATTV
     TGLAVVDTGT QFTVFGQTVI MGLIQIGGLG FMTFAVLIVM ILGKKIGLKE RMLVQEALNQ
     PTIGGVIGLV KVLFLFSISI ELIAALILSI RLVPQYGWSS GLFASLFHAI SAFNNAGFSL
     WPDNLMSYVG DPTVNLVITF LFITGGIGFT VLFDVMKNRR FKTFSLHTKL MLTGTLMLNA
     IAMLTVFILE YSNPGTLGHL HIVDKLWASY FQAVTPRTAG FNSLDFGSMR EGTIVFTLLL
     MFIGAGSAST ASGIKLTTFI VILTSVIAYL RGKKETVIFR RSIKYPIIIK ALAVSVTSLF
     IVFLGIFALT ITEQAPFLQI VFETFSAFGT VGLTMGLTPE LTTAGKCIII VIMFIGRIGP
     LTFVFSFAKT EQSNIRYPDG EVFTG
//
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