KHTU_BACSU
ID KHTU_BACSU Reviewed; 405 AA.
AC O07536; Q796V7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=K(+)/H(+) antiporter subunit KhtU {ECO:0000305};
GN Name=khtU {ECO:0000303|PubMed:24330391}; Synonyms=yhaU;
GN OrderedLocusNames=BSU09850;
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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION,
RP IDENTIFICATION OF THE KHTSTU 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 AS AN ANTIPORTER, ACTIVITY REGULATION, 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 IN METHYLGLYOXAL RESISTANCE, AND DISRUPTION PHENOTYPE.
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: Potassium/proton antiporter that mediates the efflux of
CC potassium ions from the cell (PubMed:17679694). Can also mediate
CC rubidium/proton antiport, but has no permeability for sodium or lithium
CC ions. In the absence of KhtT, does not have antiport activity, but can
CC catalyze potassium efflux (PubMed:14987767, PubMed:17679694). Involved
CC in protection of the cell from methylglyoxal, a toxic by-product of
CC glycolysis, via activation by S-lactoyl-BSH of the antiporter activity,
CC leading to cytoplasmic acidification and methylglyoxal resistance
CC (PubMed:24330391). {ECO:0000269|PubMed:14987767,
CC ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:24330391}.
CC -!- ACTIVITY REGULATION: Potassium antiport activity requires the presence
CC of KhtT. Activity is also modulated by KhtS. Has higher activity at
CC alkaline pH. {ECO:0000269|PubMed:14987767,
CC ECO:0000269|PubMed:17679694}.
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 Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Part of the khtSTU operon. Induced by salt stress at
CC alkaline pH. {ECO:0000269|PubMed:14987767}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is more sensitive to
CC methylglyoxal than wild-type. {ECO:0000269|PubMed:24330391}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y14080; CAA74453.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12825.2; -; Genomic_DNA.
DR PIR; G69819; G69819.
DR RefSeq; NP_388866.2; NC_000964.3.
DR RefSeq; WP_003233272.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07536; -.
DR SMR; O07536; -.
DR STRING; 224308.BSU09850; -.
DR TCDB; 2.A.37.5.2; the monovalent cation:proton antiporter-2 (cpa2) family.
DR PaxDb; O07536; -.
DR PRIDE; O07536; -.
DR EnsemblBacteria; CAB12825; CAB12825; BSU_09850.
DR GeneID; 939761; -.
DR KEGG; bsu:BSU09850; -.
DR PATRIC; fig|224308.179.peg.1057; -.
DR eggNOG; COG0475; Bacteria.
DR InParanoid; O07536; -.
DR OMA; MEKFFVV; -.
DR PhylomeDB; O07536; -.
DR BioCyc; BSUB:BSU09850-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:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..405
FT /note="K(+)/H(+) antiporter subunit KhtU"
FT /id="PRO_0000360834"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 43637 MW; 4C76AEABA3A685A7 CRC64;
MDHLVFEVGT ALVLVAIASV IANKIKFSII PFLIVLGMLV GPHAPKMGII DLTFIQSSEI
IEFFGRMGVL FLLFYLGLEF SVGKLIKSGK SIAVGGTIYI LINFSLGLLY GFITGFSFLE
VLILAGVITI SSSAIVAKVL VDLKRTANPE TELILGIIMF EDIFLAVYLS VVSGLILGDA
TSVGSALLSI LIAFGYMLLF FIAARKLPPL LNKLLDIRSN EVFIIVIFAA LFFIAGFSET
IHVAEAIGAL LLGLVFSETE HSDRIEHLVV PFRDFFGAMF FFSFGLSIDP FSLGEAVWLA
LGAVILTILG NFIAGMVAGR RAGLSHKASS NIGLTIVSRG EFSIIVANLG IAGGLSATLK
PFAALYVLIL AILGPLVTKE SKRIYRLLNK VFKWKPEVQP AKKQG
