RAMR_STRCO
ID RAMR_STRCO Reviewed; 202 AA.
AC Q7AKE4; Q53820;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Response regulator RamR {ECO:0000303|PubMed:12453210};
DE AltName: Full=Transcriptional activator RamR {ECO:0000303|PubMed:12453210};
GN Name=ramR {ECO:0000303|PubMed:8206859}; OrderedLocusNames=SCO6685;
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 FUNCTION.
RC STRAIN=A3(2) / M130;
RX PubMed=8206859; DOI=10.1128/jb.176.12.3800-3811.1994;
RA Ma H., Kendall K.;
RT "Cloning and analysis of a gene cluster from Streptomyces coelicolor that
RT causes accelerated aerial mycelium formation in Streptomyces lividans.";
RL J. Bacteriol. 176:3800-3811(1994).
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).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12100547; DOI=10.1046/j.1365-2958.2002.03004.x;
RA O'Connor T.J., Kanellis P., Nodwell J.R.;
RT "The ramC gene is required for morphogenesis in Streptomyces coelicolor and
RT expressed in a cell type-specific manner under the direct control of
RT RamR.";
RL Mol. Microbiol. 45:45-57(2002).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-56, AND
RP DNA-BINDING.
RC STRAIN=A3(2) / J1501;
RX PubMed=12453210; DOI=10.1046/j.1365-2958.2002.03255.x;
RA Nguyen K.T., Willey J.M., Nguyen L.D., Nguyen L.T., Viollier P.H.,
RA Thompson C.J.;
RT "A central regulator of morphological differentiation in the multicellular
RT bacterium Streptomyces coelicolor.";
RL Mol. Microbiol. 46:1223-1238(2002).
RN [5]
RP FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-12; ASP-56; THR-84; LEU-102
RP AND LYS-105, AND DNA-BINDING.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16051268; DOI=10.1016/j.jmb.2005.06.053;
RA O'Connor T.J., Nodwell J.R.;
RT "Pivotal roles for the receiver domain in the mechanism of action of the
RT response regulator RamR of Streptomyces coelicolor.";
RL J. Mol. Biol. 351:1030-1047(2005).
RN [6]
RP FUNCTION, AND REGULON.
RC STRAIN=A3(2) / J1501;
RX PubMed=16925552; DOI=10.1111/j.1365-2958.2006.05304.x;
RA San Paolo S., Huang J., Cohen S.N., Thompson C.J.;
RT "rag genes: novel components of the RamR regulon that trigger morphological
RT differentiation in Streptomyces coelicolor.";
RL Mol. Microbiol. 61:1167-1186(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / M600;
RX PubMed=17462011; DOI=10.1111/j.1365-2958.2007.05674.x;
RA Capstick D.S., Willey J.M., Buttner M.J., Elliot M.A.;
RT "SapB and the chaplins: connections between morphogenetic proteins in
RT Streptomyces coelicolor.";
RL Mol. Microbiol. 64:602-613(2007).
RN [8]
RP INDUCTION.
RC STRAIN=A3(2) / M600;
RX PubMed=22486809; DOI=10.1111/j.1365-2958.2012.08041.x;
RA Gaskell A.A., Giovinazzo J.A., Fonte V., Willey J.M.;
RT "Multi-tier regulation of the streptomycete morphogenetic peptide SapB.";
RL Mol. Microbiol. 84:501-515(2012).
CC -!- FUNCTION: A transcription factor required for aerial hyphae formation
CC on rich medium (PubMed:12100547, PubMed:12453210). Activates
CC transcription of ramC. Might be part of a two-component regulatory
CC system (PubMed:12453210). Binds the promoter of ramC (PubMed:12100547,
CC PubMed:12453210). Non-phosphorylated protein cooperatively binds
CC multiple sites in the ramC promoter. Has not been seen to
CC autophosphorylate using the small molecule phosphodonors
CC phosphoramidate, acetyl phosphate or carbamoyl phosphate
CC (PubMed:16051268). Upon low expression suppresses the bald (bld, no
CC aerial hyphae) phenotype of citA but not bldJ mutants; higher
CC expression also suppresses the bldJ mutant as well as several other bld
CC mutations, inducing SapB production even on media where SapB is
CC normally not produced (PubMed:12453210). Expression of the ram locus
CC (ramA, ramB and ramR) induces rapid aerial mycelium formation in
CC S.lividans (PubMed:8206859). Overexpression suppresses the no aerial
CC hyphae phenotype of a chaplin-negative strain, probably by inducing
CC expression of SapB (PubMed:17462011). Overexpression of RamR show there
CC are about 280 genes having at least a threefold increase or fourfold
CC decrease in RNA abundance versus wild-type including gene cluster
CC SCO4072-SCO4075 (PubMed:16925552). {ECO:0000269|PubMed:12100547,
CC ECO:0000269|PubMed:12453210, ECO:0000269|PubMed:16051268,
CC ECO:0000269|PubMed:16925552, ECO:0000269|PubMed:17462011,
CC ECO:0000269|PubMed:8206859}.
CC -!- SUBUNIT: Homodimer, in the absence of phosphorylation.
CC {ECO:0000269|PubMed:16051268}.
CC -!- INDUCTION: Transcription about 8-10 hours before aerial hyphae
CC formation commences, peaks at 38 hours just before aerial hyphae
CC formation starts, decreases rapidly and stops as sporulation commences
CC about 70 hours. Not autoregulated. {ECO:0000269|PubMed:12453210,
CC ECO:0000269|PubMed:22486809}.
CC -!- DOMAIN: The N-terminal response regulatory domain is atypical as it
CC does not have conserved residues usually found in these domains; it is
CC required for both homodimerization and DNA-binding. The C-terminal
CC domain does not bind DNA alone, nor does it form homodimers. At very
CC high concentrations overexpression of the C-terminal domain has a
CC dominant-negative effect on DNA-binding by the whole protein.
CC {ECO:0000269|PubMed:16051268}.
CC -!- PTM: May be phosphorylated by an unknown kinase, probably on Asp-56.
CC {ECO:0000305|PubMed:12453210, ECO:0000305|PubMed:16051268}.
CC -!- DISRUPTION PHENOTYPE: Deletion of ramR leads to loss of aerial hyphae
CC and sporulation on rich solid medium after 4 days growth; by 5 days
CC aerial hyphae and RamC are expressed (PubMed:12100547,
CC PubMed:12453210). Deletion on rich medium leads to an initially bald
CC (bld, no aerial hyphae) phenotype; after 4 days develops a substantial
CC aerial mycelium. Wild-type mycelium on minimal medium
CC (PubMed:17462011). No expression of SapB, normal expression of
CC chaplins. A complete chaplin-negative plus ram-negative strain
CC (deletion of ramR or the ramC-ramS-ramA-ramB operon) leads to the
CC complete loss of robust aerial hyphae (PubMed:17462011).
CC {ECO:0000269|PubMed:12100547, ECO:0000269|PubMed:12453210,
CC ECO:0000269|PubMed:17462011}.
CC -!- CAUTION: It is uncertain if Met-1 or Met-4 is the initiator.
CC {ECO:0000305|PubMed:12453210}.
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; U03771; AAA21390.1; -; Genomic_DNA.
DR EMBL; AL939128; CAD55386.1; -; Genomic_DNA.
DR PIR; T35545; T35545.
DR RefSeq; NP_733711.1; NC_003888.3.
DR RefSeq; WP_011031103.1; NZ_CP042324.1.
DR AlphaFoldDB; Q7AKE4; -.
DR SMR; Q7AKE4; -.
DR STRING; 100226.SCO6685; -.
DR GeneID; 1102124; -.
DR KEGG; sco:SCO6685; -.
DR PATRIC; fig|100226.15.peg.6790; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_0_11; -.
DR InParanoid; Q7AKE4; -.
DR OMA; VRNYMAT; -.
DR PhylomeDB; Q7AKE4; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..202
FT /note="Response regulator RamR"
FT /id="PRO_0000445443"
FT DOMAIN 135..200
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 159..178
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT REGION 1..121
FT /note="Response regulatory"
FT /evidence="ECO:0000305|PubMed:16051268"
FT MUTAGEN 12
FT /note="D->A: Restores aerial hyphae formation in ramR
FT deletion mutants, activates RamC expression."
FT /evidence="ECO:0000269|PubMed:16051268"
FT MUTAGEN 56
FT /note="D->A: Does not restore aerial hyphae formation in
FT ramR deletion mutants. Does not activate RamC expression,
FT does not bind ramC promoter, does not form homodimers."
FT /evidence="ECO:0000269|PubMed:12453210,
FT ECO:0000269|PubMed:16051268"
FT MUTAGEN 56
FT /note="D->E: Restores aerial hyphae formation in ramR
FT deletion mutants, does not bind ramC promoter."
FT /evidence="ECO:0000269|PubMed:12453210"
FT MUTAGEN 56
FT /note="D->N: Does not restore aerial hyphae formation in
FT ramR deletion mutants, does not bind ramC promoter, forms
FT homodimers."
FT /evidence="ECO:0000269|PubMed:16051268"
FT MUTAGEN 84
FT /note="T->A,I: Restores aerial hyphae formation in ramR
FT deletion mutants, activates RamC expression."
FT /evidence="ECO:0000269|PubMed:16051268"
FT MUTAGEN 102
FT /note="L->A,W: Does not restore aerial hyphae formation in
FT ramR deletion mutants, does not activate RamC expression.
FT Has lost cooperative binding to the ramC promoter, binds
FT only the high affinity site, forms homodimers."
FT /evidence="ECO:0000269|PubMed:16051268"
FT MUTAGEN 102
FT /note="L->Y: Restores aerial hyphae formation in ramR
FT deletion mutants, activates RamC expression."
FT /evidence="ECO:0000269|PubMed:16051268"
FT MUTAGEN 105
FT /note="K->A: Does not restore aerial hyphae formation in
FT ramR deletion mutants, does not activate RamC expression,
FT does not bind ramC promoter, does not form homodimers."
FT /evidence="ECO:0000269|PubMed:16051268"
SQ SEQUENCE 202 AA; 21490 MW; E8D785D4BFCC5E2D CRC64;
MGEMVRIAVV HDEKLLRSAL VQLLRSDDTL DVSSHCLDAD GPELSAALPA DVCVVDGECL
TGPEDAGAGR LRARYGDRLV VLATAKRPGV LRRAFDGGAL GLVDKNAPAH RLITAVHTVA
RGERFLDETL TVALLKGAEM PLTTRELGVL TLASQGAPIA EIAARLHLSR GTVRNYMATA
VRKVGARNRV DAIRIVQSAG WT
