DASR_STRCO
ID DASR_STRCO Reviewed; 254 AA.
AC Q9K492;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=HTH-type transcriptional repressor DasR;
GN Name=dasR; OrderedLocusNames=SCO5231; ORFNames=SC7E4.28c;
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 [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).
RN [2]
RP ROLE IN THE REGULATION OF THE PTS REGULON.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=15247334; DOI=10.1093/nar/gkh673;
RA Rigali S., Schlicht M., Hoskisson P., Nothaft H., Merzbacher M., Joris B.,
RA Titgemeyer F.;
RT "Extending the classification of bacterial transcription factors beyond the
RT helix-turn-helix motif as an alternative approach to discover new cis/trans
RT relationships.";
RL Nucleic Acids Res. 32:3418-3426(2004).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16925557; DOI=10.1111/j.1365-2958.2006.05319.x;
RA Rigali S., Nothaft H., Noens E.E.E., Schlicht M., Colson S., Mueller M.,
RA Joris B., Koerten H.K., Hopwood D.A., Titgemeyer F., van Wezel G.P.;
RT "The sugar phosphotransferase system of Streptomyces coelicolor is
RT regulated by the GntR-family regulator DasR and links N-acetylglucosamine
RT metabolism to the control of development.";
RL Mol. Microbiol. 61:1237-1251(2006).
RN [4]
RP FUNCTION IN REGULATION OF DASABC, AND INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=17351098; DOI=10.1128/aem.02612-06;
RA Saito A., Shinya T., Miyamoto K., Yokoyama T., Kaku H., Minami E.,
RA Shibuya N., Tsujibo H., Nagata Y., Ando A., Fujii T., Miyashita K.;
RT "The dasABC gene cluster, adjacent to dasR, encodes a novel ABC transporter
RT for the uptake of N,N'-diacetylchitobiose in Streptomyces coelicolor
RT A3(2).";
RL Appl. Environ. Microbiol. 73:3000-3008(2007).
RN [5]
RP REGULATION OF THE CHITINOLYTIC SYSTEM.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=17183212; DOI=10.1159/000096460;
RA Colson S., Stephan J., Hertrich T., Saito A., van Wezel G.P.,
RA Titgemeyer F., Rigali S.;
RT "Conserved cis-acting elements upstream of genes composing the chitinolytic
RT system of streptomycetes are DasR-responsive elements.";
RL J. Mol. Microbiol. Biotechnol. 12:60-66(2007).
RN [6]
RP FUNCTION IN REGULATION OF NGCEFG.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=30089751; DOI=10.1264/jsme2.me17172;
RA Iinuma C., Saito A., Ohnuma T., Tenconi E., Rosu A., Colson S.,
RA Mizutani Y., Liu F., Swiatek-Polatynska M., van Wezel G.P., Rigali S.,
RA Fujii T., Miyashita K.;
RT "NgcESco acts as a lower-affinity binding protein of an ABC transporter for
RT the uptake of N,N'-diacetylchitobiose in Streptomyces coelicolor A3(2).";
RL Microbes Environ. 33:272-281(2018).
CC -!- FUNCTION: Global regulator that is part of the nutrient-sensing system.
CC In the absence of glucosamine 6-P (GlcN6P), represses the
CC phosphotransferase system (PTS) specific for the uptake of N-
CC acetylglucosamine (PTSNag), and genes involved in the metabolism of
CC chitin, as well as several genes involved in development, thereby
CC linking carbon availability to morphogenesis (PubMed:15247334,
CC PubMed:16925557). Also regulates the expression of the ABC transporters
CC DasABC and NgcEFG, which are involved in N,N'-diacetylchitobiose
CC ((GlcNAc)2) uptake (PubMed:17351098, PubMed:30089751). Binds to the DNA
CC consensus sequence 5'-ACTGGTCTAGACCACT-3' (PubMed:15247334,
CC PubMed:16925557). {ECO:0000269|PubMed:15247334,
CC ECO:0000269|PubMed:16925557, ECO:0000269|PubMed:17351098,
CC ECO:0000269|PubMed:30089751}.
CC -!- ACTIVITY REGULATION: Binding to the target genes is abolished by
CC GlcN6P, a central molecule in N-acetylglucosamine metabolism.
CC {ECO:0000269|PubMed:16925557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by (GlcNAc)2 and (GlcNAc)3.
CC {ECO:0000269|PubMed:17351098}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a bald phenotype,
CC mutant fails to produce aerial hyphae and spores on glucose-containig
CC media. The mutant is arrested at an early stage of the developmental
CC program. {ECO:0000269|PubMed:16925557}.
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DR EMBL; AL939123; CAB94616.1; -; Genomic_DNA.
DR RefSeq; NP_629378.1; NC_003888.3.
DR RefSeq; WP_003973740.1; NZ_VNID01000008.1.
DR PDB; 4ZS8; X-ray; 2.60 A; A/B=1-254.
DR PDB; 4ZSB; X-ray; 2.00 A; A=89-254.
DR PDB; 4ZSI; X-ray; 1.65 A; A/B=88-254.
DR PDB; 4ZSK; X-ray; 1.85 A; A/B=88-254.
DR PDBsum; 4ZS8; -.
DR PDBsum; 4ZSB; -.
DR PDBsum; 4ZSI; -.
DR PDBsum; 4ZSK; -.
DR AlphaFoldDB; Q9K492; -.
DR SMR; Q9K492; -.
DR STRING; 100226.SCO5231; -.
DR GeneID; 1100672; -.
DR KEGG; sco:SCO5231; -.
DR PATRIC; fig|100226.15.peg.5314; -.
DR eggNOG; COG2188; Bacteria.
DR HOGENOM; CLU_063236_2_3_11; -.
DR InParanoid; Q9K492; -.
DR OMA; DRYKFVA; -.
DR PhylomeDB; Q9K492; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.1410.10; -; 1.
DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR011663; UTRA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00392; GntR; 1.
DR Pfam; PF07702; UTRA; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SMART; SM00866; UTRA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF64288; SSF64288; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..254
FT /note="HTH-type transcriptional repressor DasR"
FT /id="PRO_0000281408"
FT DOMAIN 17..87
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 47..66
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:4ZS8"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4ZS8"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:4ZS8"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4ZS8"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4ZS8"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4ZS8"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4ZS8"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4ZSI"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:4ZSI"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:4ZSI"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4ZSI"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4ZSI"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4ZSI"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 188..199
FT /evidence="ECO:0007829|PDB:4ZSI"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 214..225
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:4ZSI"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4ZSI"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:4ZSI"
SQ SEQUENCE 254 AA; 28344 MW; 30EE05627021E378 CRC64;
MSTDVSSAEN EGGATVRTAR VPKYYRLKKH LLDMTRTQTP GTPVPPERTL AAEFDTSRTT
VRQALQELVV EGRLERIQGK GTFVAKPKVS QALQLTSYTE DMRAQGLEPT SQLLDIGYIT
ADDRLAGLLD ITAGGRVLRI ERLRMANGEP MAIETTHLSA KRFPALRRSL VKYTSLYTAL
AEVYDVHLAE AEETIETSLA TPREAGLLGT DVGLPMLMLS RHSQDRTGQP VEWVRSVYRG
DRYKFVARLK RPQD
