KHTT_BACSU
ID KHTT_BACSU Reviewed; 165 AA.
AC O07535; Q796V6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=K(+)/H(+) antiporter subunit KhtT {ECO:0000305};
GN Name=khtT {ECO:0000303|PubMed:24330391}; Synonyms=yhaT;
GN OrderedLocusNames=BSU09860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [2]
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 [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION OF THE KHTSTU
RP OPERON, AND INDUCTION.
RX PubMed=14987767; DOI=10.1016/s0378-1097(03)00959-5;
RA Fujisawa M., Wada Y., Ito M.;
RT "Modulation of the K+ efflux activity of Bacillus subtilis YhaU by YhaT and
RT the C-terminal region of YhaS.";
RL FEMS Microbiol. Lett. 231:211-217(2004).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17679694; DOI=10.1073/pnas.0703709104;
RA Fujisawa M., Ito M., Krulwich T.A.;
RT "Three two-component transporters with channel-like properties have
RT monovalent cation/proton antiport activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13289-13294(2007).
RN [5]
RP FUNCTION.
RX PubMed=24330391; DOI=10.1111/mmi.12489;
RA Chandrangsu P., Dusi R., Hamilton C.J., Helmann J.D.;
RT "Methylglyoxal resistance in Bacillus subtilis: contributions of
RT bacillithiol-dependent and independent pathways.";
RL Mol. Microbiol. 91:706-715(2014).
CC -!- FUNCTION: Required for activity of the potassium/proton antiporter KhtU
CC (PubMed:14987767, PubMed:17679694). Involved in protection of the cell
CC from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).
CC {ECO:0000269|PubMed:14987767, ECO:0000269|PubMed:17679694,
CC ECO:0000269|PubMed:24330391}.
CC -!- SUBUNIT: The transporter is composed of the integral membrane protein
CC KhtU and the regulatory protein KhtT. {ECO:0000269|PubMed:14987767,
CC ECO:0000269|PubMed:17679694}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:14987767};
CC Peripheral membrane protein {ECO:0000305|PubMed:14987767}; Cytoplasmic
CC side {ECO:0000305|PubMed:14987767}.
CC -!- INDUCTION: Part of the khtSTU operon. Induced by salt stress at
CC alkaline pH. {ECO:0000269|PubMed:14987767}.
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DR EMBL; Y14080; CAA74452.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12826.1; -; Genomic_DNA.
DR PIR; F69819; F69819.
DR RefSeq; NP_388867.1; NC_000964.3.
DR RefSeq; WP_003233269.1; NZ_JNCM01000035.1.
DR PDB; 7AGV; X-ray; 1.85 A; A/B/C/D/E/F/G/H=2-165.
DR PDB; 7AGW; X-ray; 1.51 A; A/B=2-68.
DR PDB; 7AGY; X-ray; 1.54 A; A/B=2-68.
DR PDB; 7AHM; X-ray; 3.14 A; A/B/C/D=2-165.
DR PDB; 7AHT; X-ray; 2.16 A; A/B=2-68.
DR PDBsum; 7AGV; -.
DR PDBsum; 7AGW; -.
DR PDBsum; 7AGY; -.
DR PDBsum; 7AHM; -.
DR PDBsum; 7AHT; -.
DR AlphaFoldDB; O07535; -.
DR SMR; O07535; -.
DR STRING; 224308.BSU09860; -.
DR TCDB; 2.A.37.5.2; the monovalent cation:proton antiporter-2 (cpa2) family.
DR PaxDb; O07535; -.
DR PRIDE; O07535; -.
DR EnsemblBacteria; CAB12826; CAB12826; BSU_09860.
DR GeneID; 936284; -.
DR KEGG; bsu:BSU09860; -.
DR PATRIC; fig|224308.179.peg.1058; -.
DR eggNOG; COG0490; Bacteria.
DR InParanoid; O07535; -.
DR OMA; EGAYFQP; -.
DR PhylomeDB; O07535; -.
DR BioCyc; BSUB:BSU09860-MON; -.
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:0006813; P:potassium ion transport; IEA:InterPro.
DR Gene3D; 3.30.70.1450; -; 1.
DR InterPro; IPR026278; K(+)/H(+)_antiporter_KhtT.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR Pfam; PF02080; TrkA_C; 1.
DR PIRSF; PIRSF005028; KhtT; 1.
DR SUPFAM; SSF116726; SSF116726; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome.
FT CHAIN 1..165
FT /note="K(+)/H(+) antiporter subunit KhtT"
FT /id="PRO_0000360835"
FT DOMAIN 76..161
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7AGW"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:7AGW"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:7AGW"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:7AGW"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:7AGW"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:7AGW"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:7AGW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7AGV"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7AGV"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7AGV"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:7AGV"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:7AGV"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:7AGV"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:7AGV"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:7AHM"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:7AGV"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7AGV"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:7AGV"
SQ SEQUENCE 165 AA; 18729 MW; 5E28A8A6F0DA9C59 CRC64;
MNIKENDLPG IGKKFEIETR SHEKMTIIIH DDGRREIYRF NDRDPDELLS NISLDDSEAR
QIAAILGGMV YKPQALESIE MAFSDLIIEW FKVEKGAKSI GRTLGELDVR QNYDVTVIAI
IKHNQEKLLN PGADSIIEEN DTLVLSGERK HLKKLIHDFL SGEGV
