ID   SPAR_BACIU              Reviewed;         220 AA.
AC   P33112;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Transcriptional regulatory protein SpaR;
DE   AltName: Full=Subtilin biosynthesis regulatory protein SpaR;
GN   Name=spaR;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=8439156; DOI=10.1128/aem.59.1.296-303.1993;
RA   Klein C., Kaletta C., Entian K.-D.;
RT   "Biosynthesis of the lantibiotic subtilin is regulated by a histidine
RT   kinase/response regulator system.";
RL   Appl. Environ. Microbiol. 59:296-303(1993).
CC   -!- FUNCTION: Member of the two-component regulatory system SpaK/SpaR
CC       involved in the regulation of the biosynthesis of lantibiotic subtilin.
CC       SpaR may function as a regulatory protein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylated by SpaK. {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; L07785; AAA22780.1; -; Genomic_DNA.
DR   EMBL; U09819; AAB91594.1; -; Genomic_DNA.
DR   PIR; A48965; A48965.
DR   RefSeq; WP_003220039.1; NZ_ML241279.1.
DR   AlphaFoldDB; P33112; -.
DR   SMR; P33112; -.
DR   DIP; DIP-48346N; -.
DR   IntAct; P33112; 1.
DR   GeneID; 64305131; -.
DR   PATRIC; fig|1423.172.peg.2879; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..220
FT                   /note="Transcriptional regulatory protein SpaR"
FT                   /id="PRO_0000081225"
FT   DOMAIN          3..115
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        124..220
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         51
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   220 AA;  25615 MW;  0C0E1406122FF029 CRC64;
     MAKILAVDDE KDILVLIQNI LRRDQHQVDI LDHVHGQPPD VFQGYDLILL DVMMPDIDGF
     ELCKQIRPLV DCPILFLTAK TEEEAIVKGL ITGGDDYITK PFGVRELSAR VNAHLRRERR
     DKHQSKRVIS GFLFHFDSKE VFINNNKLNL TKNEYKICEF LAQHKGRTFS REQIYEEIYG
     LEGNALYSTI TEFIRTIRKK CKEHNADPIK TVWGVGYKWE