YXDK_BACSU
ID YXDK_BACSU Reviewed; 325 AA.
AC P42422;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sensor histidine kinase YxdK;
DE EC=2.7.13.3;
GN Name=yxdK; OrderedLocusNames=BSU39650; ORFNames=B65E;
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 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-325.
RC STRAIN=168 / BGSC1A1;
RX PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT between the iol and hut operons.";
RL DNA Res. 2:295-301(1995).
RN [4]
RP FUNCTION.
RX PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA Fujita Y.;
RT "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT regulatory systems.";
RL J. Bacteriol. 183:7365-7370(2001).
RN [5]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=15870467; DOI=10.1099/mic.0.27761-0;
RA Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M.,
RA Kontinen V.P.;
RT "Cationic antimicrobial peptides elicit a complex stress response in
RT Bacillus subtilis that involves ECF-type sigma factors and two-component
RT signal transduction systems.";
RL Microbiology 151:1577-1592(2005).
CC -!- FUNCTION: Probable member of the two-component regulatory system
CC YxdK/YxdJ. May activate YxdJ in response to the antibacterial protein
CC LL-37. {ECO:0000269|PubMed:11717295, ECO:0000269|PubMed:15870467}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14399; BAA03301.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16001.1; -; Genomic_DNA.
DR EMBL; D45912; BAA08314.1; -; Genomic_DNA.
DR PIR; H70073; H70073.
DR RefSeq; NP_391844.1; NC_000964.3.
DR RefSeq; WP_003243885.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42422; -.
DR SMR; P42422; -.
DR STRING; 224308.BSU39650; -.
DR PaxDb; P42422; -.
DR PRIDE; P42422; -.
DR DNASU; 937487; -.
DR EnsemblBacteria; CAB16001; CAB16001; BSU_39650.
DR GeneID; 937487; -.
DR KEGG; bsu:BSU39650; -.
DR PATRIC; fig|224308.179.peg.4290; -.
DR eggNOG; COG2205; Bacteria.
DR InParanoid; P42422; -.
DR OMA; LNHEVEI; -.
DR PhylomeDB; P42422; -.
DR BioCyc; BSUB:BSU39650-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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..325
FT /note="Sensor histidine kinase YxdK"
FT /id="PRO_0000074923"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 118..325
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 121
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 325 AA; 37989 MW; 9078D6540BA42914 CRC64;
MKLFLRSHAV LILLFLLQGL FVFFYYWFAG LHSFSHLFYI LGVQLLILAG YLAYRWYKDR
GVYHWLSSGQ EGTDIPYLGS SVFCSELYEK QMELIRLQHQ KLHETEAKLD ARVTYMNQWV
HQVKTPLSVI NLIIQEEDEP VFEQIKKEVR QIEFGLETLL YSSRLDLFER DFKIEAVSLS
ELLQSVIQSY KRFFIQYRVY PKMNVCDDHQ IYTDAKWLKF AIGQVVTNAV KYSAGKSDRL
ELNVFCDEDR TVLEVKDYGV GIPSQDIKRV FDPYYTGENG RRFQESTGIG LHLVKEITDK
LNHTVDISSS PGEGTSVRFS FLTKM
