ID   AFSQ1_STRCO             Reviewed;         225 AA.
AC   Q04942; Q9AK20;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Transcriptional regulatory protein AfsQ1;
GN   Name=afsQ1; OrderedLocusNames=SCO4907; ORFNames=2SCK8.33c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ASP-52.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=1339426; DOI=10.1128/jb.174.23.7585-7594.1992;
RA   Ishizuka H., Horinouchi S., Kieser H.M., Hopwood D.A., Beppu T.;
RT   "A putative two-component regulatory system involved in secondary
RT   metabolism in Streptomyces spp.";
RL   J. Bacteriol. 174:7585-7594(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Forms part of a two-component regulatory system AfsQ1/AfsQ2
CC       involved in secondary metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylated by AfsQ2. {ECO:0000305}.
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DR   EMBL; D10654; BAA01502.1; -; Genomic_DNA.
DR   EMBL; AL939121; CAC33072.1; -; Genomic_DNA.
DR   PIR; A45270; A45270.
DR   RefSeq; NP_629060.1; NC_003888.3.
DR   RefSeq; WP_003974066.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; Q04942; -.
DR   SMR; Q04942; -.
DR   STRING; 100226.SCO4907; -.
DR   GeneID; 1100348; -.
DR   KEGG; sco:SCO4907; -.
DR   PATRIC; fig|100226.15.peg.4986; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_4_11; -.
DR   InParanoid; Q04942; -.
DR   OMA; RSFIVIN; -.
DR   PhylomeDB; Q04942; -.
DR   Proteomes; UP000001973; 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   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; 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; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..225
FT                   /note="Transcriptional regulatory protein AfsQ1"
FT                   /id="PRO_0000080993"
FT   DOMAIN          3..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        124..223
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         52
FT                   /note="D->E: Loss of protein's ability to stimulate
FT                   antibiotic production and pigmentation."
FT                   /evidence="ECO:0000269|PubMed:1339426"
FT   CONFLICT        11
FT                   /note="D -> E (in Ref. 1; BAA01502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   225 AA;  25107 MW;  2834669A9F3F1E3E CRC64;
     MPSLLLIEDD DAIRTALELS LTRQGHRVAT AASGEDGLKL LREQRPDLIV LDVMLPGIDG
     FEVCRRIRRT DQLPIILLTA RNDDIDVVVG LESGADDYVV KPVQGRVLDA RIRAVLRRGE
     RESTDSASFG SLVIDRSAMT VTKNGEDLQL TPTELRLLLE LSRRPGQALS RQQLLRLVWE
     HDYLGDSRLV DACVQRLRAK VEDVPSSPTL IRTVRGVGYR LDPPQ