WALR_BACSU
ID WALR_BACSU Reviewed; 235 AA.
AC P37478;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transcriptional regulatory protein WalR {ECO:0000305};
GN Name=walR {ECO:0000250|UniProtKB:Q2G2U6, ECO:0000312|EMBL:CAB16078.1};
GN Synonyms=yycF; OrderedLocusNames=BSU40410;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND MUTAGENESIS OF HIS-215.
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 [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-53.
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 [6]
RP PHOSPHORYLATION.
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 [7]
RP MUTAGENESIS OF HIS-215, AND SUBUNIT.
RX PubMed=15153768; DOI=10.1159/000077246;
RA Watanabe T., Hashimoto Y., Umemoto Y., Tatebe D., Furuta E., Fukamizo T.,
RA Yamamoto K., Utsumi R.;
RT "Molecular characterization of the essential response regulator protein
RT YycF in Bacillus subtilis.";
RL J. Mol. Microbiol. Biotechnol. 6:155-163(2003).
RN [8]
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 [9]
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, ykvT, cwlO,
CC lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons. Binds to
CC the ftsAZ P1 promoter sequence in vitro. WalR has been shown to
CC directly bind to the regulatory regions of yocH, ykvT, tagAB/tagDEF.
CC Activates cwlO, lytE and ydjM and represses yoeB and yjeA.
CC {ECO:0000269|PubMed:10878122, ECO:0000269|PubMed:12950927,
CC ECO:0000269|PubMed:17581128, ECO:0000269|PubMed:9829949}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15153768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during exponential growth and shut down
CC at the entry into stationary phase.
CC -!- PTM: Phosphorylated by WalK. {ECO:0000269|PubMed:11758928}.
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DR EMBL; D26185; BAA05173.1; -; Genomic_DNA.
DR EMBL; D78193; BAA11300.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16078.1; -; Genomic_DNA.
DR PIR; S65967; S65967.
DR RefSeq; NP_391921.1; NC_000964.3.
DR RefSeq; WP_003244363.1; NZ_JNCM01000034.1.
DR PDB; 2D1V; X-ray; 2.40 A; A=128-235.
DR PDB; 2ZWM; X-ray; 2.04 A; A/B=1-122.
DR PDB; 3F6P; X-ray; 1.95 A; A=1-120.
DR PDBsum; 2D1V; -.
DR PDBsum; 2ZWM; -.
DR PDBsum; 3F6P; -.
DR AlphaFoldDB; P37478; -.
DR SMR; P37478; -.
DR STRING; 224308.BSU40410; -.
DR jPOST; P37478; -.
DR PaxDb; P37478; -.
DR PRIDE; P37478; -.
DR EnsemblBacteria; CAB16078; CAB16078; BSU_40410.
DR GeneID; 64305833; -.
DR GeneID; 937776; -.
DR KEGG; bsu:BSU40410; -.
DR PATRIC; fig|224308.179.peg.4374; -.
DR eggNOG; COG0745; Bacteria.
DR InParanoid; P37478; -.
DR OMA; IDRVWGS; -.
DR PhylomeDB; P37478; -.
DR BioCyc; BSUB:BSU40410-MON; -.
DR EvolutionaryTrace; P37478; -.
DR PRO; PR:P37478; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CACAO.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..235
FT /note="Transcriptional regulatory protein WalR"
FT /id="PRO_0000081399"
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 132..231
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MUTAGEN 53
FT /note="D->H: Constitutively active."
FT /evidence="ECO:0000269|PubMed:10878122"
FT MUTAGEN 215
FT /note="H->P: In JH17041; thermosensitive; decrease in
FT dimerization and DNA-binding."
FT /evidence="ECO:0000269|PubMed:15153768,
FT ECO:0000269|PubMed:9829949"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3F6P"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3F6P"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3F6P"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:3F6P"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3F6P"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3F6P"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:3F6P"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3F6P"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:3F6P"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3F6P"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:3F6P"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2D1V"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2D1V"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2D1V"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2D1V"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:2D1V"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2D1V"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:2D1V"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:2D1V"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2D1V"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2D1V"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2D1V"
SQ SEQUENCE 235 AA; 27226 MW; 201BC21CBB5EC6B4 CRC64;
MDKKILVVDD EKPIADILEF NLRKEGYEVH CAHDGNEAVE MVEELQPDLI LLDIMLPNKD
GVEVCREVRK KYDMPIIMLT AKDSEIDKVI GLEIGADDYV TKPFSTRELL ARVKANLRRQ
LTTAPAEEEP SSNEIHIGSL VIFPDAYVVS KRDETIELTH REFELLHYLA KHIGQVMTRE
HLLQTVWGYD YFGDVRTVDV TVRRLREKIE DNPSHPNWIV TRRGVGYYLR NPEQD
