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 03-AUG-2022, entry version 128.
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 O32080; O32080: ktrA; NbExp=2; IntAct=EBI-16045427, EBI-16045427;
CC O32080; 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}.
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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 PDB; 6S2J; X-ray; 2.67 A; A/B=1-222.
DR PDB; 6S5B; X-ray; 3.05 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 6S5C; X-ray; 3.00 A; A/B=1-222.
DR PDB; 6S5D; X-ray; 3.39 A; A/B=1-222.
DR PDB; 6S5E; X-ray; 3.89 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 6S5G; X-ray; 4.33 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 6S5N; X-ray; 4.09 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 6S5O; X-ray; 3.98 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 6S7R; X-ray; 3.73 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-222.
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 PDBsum; 6S2J; -.
DR PDBsum; 6S5B; -.
DR PDBsum; 6S5C; -.
DR PDBsum; 6S5D; -.
DR PDBsum; 6S5E; -.
DR PDBsum; 6S5G; -.
DR PDBsum; 6S5N; -.
DR PDBsum; 6S5O; -.
DR PDBsum; 6S7R; -.
DR AlphaFoldDB; O32080; -.
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; BSU_31090.
DR GeneID; 937145; -.
DR KEGG; bsu:BSU31090; -.
DR PATRIC; fig|224308.179.peg.3369; -.
DR eggNOG; COG0569; Bacteria.
DR InParanoid; O32080; -.
DR OMA; AIGANIQ; -.
DR PhylomeDB; O32080; -.
DR BioCyc; BSUB:BSU31090-MON; -.
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;
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 BINDING 16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 36..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 56..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 78..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 103..105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12086676,
FT ECO:0000269|PubMed:16990138"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2HMT"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2HMT"
FT TURN 44..48
FT /evidence="ECO:0007829|PDB:2HMT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:2HMT"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2HMT"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:2HMT"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:2HMT"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2HMT"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:2HMT"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2HMV"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4J91"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4J91"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6S2J"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6S2J"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6S2J"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6S2J"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6S2J"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:6S2J"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:6S2J"
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
