(data stored in SCRATCH zone)

SWISSPROT: KTRA_BACSU

ID   KTRA_BACSU              Reviewed;         222 AA.
AC   O32080;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Ktr system potassium uptake protein A;
DE            Short=K(+)-uptake protein KtrA;
GN   Name=ktrA; Synonyms=yuaA; OrderedLocusNames=BSU31090;
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   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-142 IN COMPLEX WITH NAD, AND
RP   SUBUNIT.
RX   PubMed=12086676; DOI=10.1016/s0092-8674(02)00768-7;
RA   Roosild T.P., Miller S., Booth I.R., Choe S.;
RT   "A mechanism of regulating transmembrane potassium flux through a ligand-
RT   mediated conformational switch.";
RL   Cell 109:781-791(2002).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-144 IN COMPLEX WITH NAD,
RP   INTERACTION WITH KTRB, 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).
CC   -!- FUNCTION: Catalytic subunit of the KtrAB potassium uptake transporter.
CC       The 2 major potassium transporter complexes KtrAB and KtrCD confer
CC       resistance to both suddenly imposed and prolonged osmotic stress.
CC       {ECO:0000269|PubMed:12562800}.
CC   -!- SUBUNIT: Homodimer, tetramer (dimer of homodimer) and octamer (tetramer
CC       of 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:12086676,
CC       ECO:0000269|PubMed:16990138}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-16045427, EBI-16045427;
CC       O32081:ktrB; NbExp=2; IntAct=EBI-16045427, EBI-16045470;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impaired potassium uptake.
CC       {ECO:0000269|PubMed:12562800}.
CC   -!- SIMILARITY: Belongs to the KtrA potassium transport family.
CC       {ECO:0000305}.
DR   EMBL; AL009126; CAB15087.1; -; Genomic_DNA.
DR   PIR; C70005; C70005.
DR   RefSeq; NP_390987.1; NC_000964.3.
DR   RefSeq; WP_003243377.1; NZ_JNCM01000033.1.
DR   PDB; 1LSU; X-ray; 2.85 A; A/B=1-143.
DR   PDB; 2HMS; X-ray; 2.70 A; A/B/C/D=1-144.
DR   PDB; 2HMT; X-ray; 2.20 A; A/B=1-144.
DR   PDB; 2HMU; X-ray; 2.25 A; A/B=1-144.
DR   PDB; 2HMV; X-ray; 2.20 A; A/B=1-144.
DR   PDB; 2HMW; X-ray; 3.00 A; A/B=1-144.
DR   PDB; 4J7C; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 4J90; X-ray; 3.24 A; A/B=1-222.
DR   PDB; 4J91; X-ray; 2.93 A; A/B/C/D=1-222.
DR   PDB; 5BUT; X-ray; 5.97 A; A/C/E/G=1-212.
DR   PDBsum; 1LSU; -.
DR   PDBsum; 2HMS; -.
DR   PDBsum; 2HMT; -.
DR   PDBsum; 2HMU; -.
DR   PDBsum; 2HMV; -.
DR   PDBsum; 2HMW; -.
DR   PDBsum; 4J7C; -.
DR   PDBsum; 4J90; -.
DR   PDBsum; 4J91; -.
DR   PDBsum; 5BUT; -.
DR   SMR; O32080; -.
DR   DIP; DIP-60209N; -.
DR   IntAct; O32080; 1.
DR   STRING; 224308.BSU31090; -.
DR   TCDB; 2.A.38.4.3; the k(+) transporter (trk) family.
DR   PaxDb; O32080; -.
DR   PRIDE; O32080; -.
DR   EnsemblBacteria; CAB15087; CAB15087; BSU31090.
DR   GeneID; 937145; -.
DR   KEGG; bsu:BSU31090; -.
DR   PATRIC; fig|224308.179.peg.3369; -.
DR   eggNOG; COG0569; LUCA.
DR   HOGENOM; HOG000279860; -.
DR   InParanoid; O32080; -.
DR   KO; K03499; -.
DR   OMA; AIGANIQ; -.
DR   PhylomeDB; O32080; -.
DR   BioCyc; BSUB:BSU31090-MONOMER; -.
DR   EvolutionaryTrace; O32080; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1450; -; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006037; RCK_C.
DR   InterPro; IPR036721; RCK_C_sf.
DR   InterPro; IPR003148; RCK_N.
DR   Pfam; PF02080; TrkA_C; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   SUPFAM; SSF116726; SSF116726; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51202; RCK_C; 1.
DR   PROSITE; PS51201; RCK_N; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O32080.
DR   SWISS-2DPAGE; O32080.
KW   3D-structure; Cell membrane; Ion transport; Membrane; NAD; Potassium;
KW   Potassium transport; Reference proteome; Transport.
FT   CHAIN           1..222
FT                   /note="Ktr system potassium uptake protein A"
FT                   /id="PRO_0000360619"
FT   DOMAIN          8..130
FT                   /note="RCK N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   DOMAIN          139..222
FT                   /note="RCK C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   NP_BIND         36..38
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   NP_BIND         56..57
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   NP_BIND         78..80
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   NP_BIND         103..105
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   BINDING         16
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   BINDING         109
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   BINDING         125
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|PubMed:12086676,
FT                   ECO:0000269|PubMed:16990138"
FT   STRAND          8..12
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           16..27
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   STRAND          33..37
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           39..43
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   TURN            44..48
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   STRAND          50..54
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           60..64
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   TURN            65..67
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           68..70
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   STRAND          72..76
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           82..94
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   STRAND          98..103
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           107..116
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   STRAND          119..122
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   HELIX           124..140
FT                   /evidence="ECO:0000244|PDB:2HMT"
FT   TURN            141..143
FT                   /evidence="ECO:0000244|PDB:2HMV"
FT   STRAND          148..151
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   STRAND          153..156
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   HELIX           160..162
FT                   /evidence="ECO:0000244|PDB:4J90"
FT   TURN            167..169
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   HELIX           172..175
FT                   /evidence="ECO:0000244|PDB:4J90"
FT   STRAND          179..185
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   STRAND          188..192
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   STRAND          205..209
FT                   /evidence="ECO:0000244|PDB:4J91"
FT   HELIX           211..221
FT                   /evidence="ECO:0000244|PDB:4J91"
SQ   SEQUENCE   222 AA;  24882 MW;  24E32EDB155E806F CRC64;
     MGRIKNKQFA VIGLGRFGGS ICKELHRMGH EVLAVDINEE KVNAYASYAT HAVIANATEE
     NELLSLGIRN FEYVIVAIGA NIQASTLTTL LLKELDIPNI WVKAQNYYHH KVLEKIGADR
     IIHPEKDMGV KIAQSLSDEN VLNYIDLSDE YSIVELLATR KLDSKSIIDL NVRAKYGCTI
     LAIKHHGDIC LSPAPEDIIR EQDCLVIMGH KKDIKRFENE GM
//

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