KTRB_BACSU
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 03-AUG-2022, entry version 108.
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 AlphaFoldDB; O32081; -.
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 PRIDE; 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-MON; -.
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
