WALK_BACSU
ID WALK_BACSU Reviewed; 611 AA.
AC Q45614;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sensor histidine kinase WalK {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:11758928};
GN Name=walK {ECO:0000250|UniProtKB:Q2G2U4, ECO:0000312|EMBL:CAB16077.1};
GN Synonyms=yycG; OrderedLocusNames=BSU40400;
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=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
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.
RC STRAIN=168 / JH642;
RX PubMed=9829949; DOI=10.1128/jb.180.23.6375-6383.1998;
RA Fabret C., Hoch J.A.;
RT "A two-component signal transduction system essential for growth of
RT Bacillus subtilis: implications for anti-infective therapy.";
RL J. Bacteriol. 180:6375-6383(1998).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=10878122; DOI=10.1099/00221287-146-7-1573;
RA Fukuchi K., Kasahara Y., Asai K., Kobayashi K., Moriya S., Ogasawara N.;
RT "The essential two-component regulatory system encoded by yycF and yycG
RT modulates expression of the ftsAZ operon in Bacillus subtilis.";
RL Microbiology 146:1573-1583(2000).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT HIS-386, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP HIS-386, AND INHIBITION BY IMIDAZOLE AND ZERUMBONE DERIVATIVES.
RX PubMed=11758928; DOI=10.1271/bbb.65.2306;
RA Yamamoto K., Kitayama T., Minagawa S., Watanabe T., Sawada S., Okamoto T.,
RA Utsumi R.;
RT "Antibacterial agents that inhibit histidine protein kinase YycG of
RT Bacillus subtilis.";
RL Biosci. Biotechnol. Biochem. 65:2306-2310(2001).
RN [6]
RP STUDY OF THE WALR/WALK REGULON.
RX PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
RA Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
RA Devine K.;
RT "Genes controlled by the essential YycG/YycF two-component system of
RT Bacillus subtilis revealed through a novel hybrid regulator approach.";
RL Mol. Microbiol. 49:1639-1655(2003).
RN [7]
RP INTERACTION WITH YYCH AND YYCI, AND SUBUNIT.
RX PubMed=17307850; DOI=10.1128/jb.01936-06;
RA Szurmant H., Mohan M.A., Imus P.M., Hoch J.A.;
RT "YycH and YycI interact to regulate the essential YycFG two-component
RT system in Bacillus subtilis.";
RL J. Bacteriol. 189:3280-3289(2007).
RN [8]
RP FUNCTION.
RX PubMed=17581128; DOI=10.1111/j.1365-2958.2007.05782.x;
RA Bisicchia P., Noone D., Lioliou E., Howell A., Quigley S., Jensen T.,
RA Jarmer H., Devine K.M.;
RT "The essential YycFG two-component system controls cell wall metabolism in
RT Bacillus subtilis.";
RL Mol. Microbiol. 65:180-200(2007).
CC -!- FUNCTION: Member of the two-component regulatory system WalK/WalR
CC involved in the regulation of the ftsAZ operon, the yocH and ykvT,
CC cwlO, lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons.
CC Phosphorylates WalR. {ECO:0000269|PubMed:10878122,
CC ECO:0000269|PubMed:11758928, ECO:0000269|PubMed:12950927,
CC ECO:0000269|PubMed:17581128, ECO:0000269|PubMed:9829949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:11758928};
CC -!- SUBUNIT: Homodimer. Interacts with YycH and YycI.
CC {ECO:0000269|PubMed:17307850}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed during exponential growth and shut down
CC at the entry into stationary phase.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11758928}.
CC -!- MISCELLANEOUS: The imidazole derivatives NH125, NH126 and NH127
CC inhibited the incorporation of phosphate from ATP at 50 ug/ml. The
CC zerumbone derivative NH0891 inhibited WalK.
CC {ECO:0000269|PubMed:11758928}.
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; D78193; BAA11299.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16077.1; -; Genomic_DNA.
DR PIR; F70089; F70089.
DR RefSeq; NP_391920.1; NC_000964.3.
DR RefSeq; WP_009968432.1; NZ_JNCM01000034.1.
DR PDB; 3SL2; X-ray; 1.61 A; A=451-611.
DR PDBsum; 3SL2; -.
DR AlphaFoldDB; Q45614; -.
DR SMR; Q45614; -.
DR IntAct; Q45614; 2.
DR STRING; 224308.BSU40400; -.
DR BindingDB; Q45614; -.
DR ChEMBL; CHEMBL1075059; -.
DR iPTMnet; Q45614; -.
DR PaxDb; Q45614; -.
DR PRIDE; Q45614; -.
DR DNASU; 937793; -.
DR EnsemblBacteria; CAB16077; CAB16077; BSU_40400.
DR GeneID; 937793; -.
DR KEGG; bsu:BSU40400; -.
DR PATRIC; fig|224308.179.peg.4373; -.
DR eggNOG; COG5002; Bacteria.
DR InParanoid; Q45614; -.
DR OMA; LTFWAVN; -.
DR PhylomeDB; Q45614; -.
DR BioCyc; BSUB:BSU40400-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR PRO; PR:Q45614; -.
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:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..611
FT /note="Sensor histidine kinase WalK"
FT /id="PRO_0000074918"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 204..256
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 263..324
FT /note="PAS"
FT /evidence="ECO:0000305"
FT DOMAIN 325..379
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 383..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 386
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:11758928"
FT MUTAGEN 386
FT /note="H->R,A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:11758928"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:3SL2"
FT HELIX 454..466
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3SL2"
FT HELIX 490..506
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:3SL2"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:3SL2"
FT TURN 540..547
FT /evidence="ECO:0007829|PDB:3SL2"
FT HELIX 567..577
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:3SL2"
FT TURN 588..590
FT /evidence="ECO:0007829|PDB:3SL2"
FT STRAND 591..601
FT /evidence="ECO:0007829|PDB:3SL2"
SQ SEQUENCE 611 AA; 70034 MW; 2E7B7CB538410AE7 CRC64;
MNKVGFFRSI QFKITLIYVL LIIIAMQIIG VYFVNQVEKS LISSYEQSLN QRIDNLSYYI
EQEYKSDNDS TVIKDDVSRI LNDFTKSDEV REISFVDKSY EVVGSSKPYG EEVAGKQTTD
LIFKRIFSTK QSYLRKYYDP KSKIRVLISA KPVMTENQEV VGAIYVVASM EDVFNQMKTI
NTILASGTGL ALVLTALLGI FLARTITHPL SDMRKQAMEL AKGNFSRKVK KYGHDEIGQL
ATTFNHLTRE LEDAQAMTEG ERRKLASVIA YMTDGVIATN RNGAIILLNS PALELLNVSR
ETALEMPITS LLGLQENYTF EDLVEQQDSM LLEIERDDEL TVLRVNFSVI QREHGKIDGL
IAVIYDVTEQ EKMDQERREF VANVSHELRT PLTTMRSYLE ALAEGAWENK DIAPRFLMVT
QNETERMIRL VNDLLQLSKF DSKDYQFNRE WIQIVRFMSL IIDRFEMTKE QHVEFIRNLP
DRDLYVEIDQ DKITQVLDNI ISNALKYSPE GGHVTFSIDV NEEEELLYIS VKDEGIGIPK
KDVEKVFDRF YRVDKARTRK LGGTGLGLAI AKEMVQAHGG DIWADSIEGK GTTITFTLPY
KEEQEDDWDE A
