Actinobacteria TFDB: An integrated view of transcription factors in Actinobacteria

Yu Fu , Zhan-Hui Xu , Yi-Fan Liang , Shi-Qi Yang , Xue-Qin Xie , Bang-Ce Ye , Di You

Engineering Microbiology ›› 2026, Vol. 6 ›› Issue (2) : 100272

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Engineering Microbiology ›› 2026, Vol. 6 ›› Issue (2) :100272 DOI: 10.1016/j.engmic.2026.100272
Original Research Article
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Actinobacteria TFDB: An integrated view of transcription factors in Actinobacteria
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Abstract

Actinobacteria represent a prolific source of bioactive natural products. However, the complex transcriptional regulatory networks in these bacteria, particularly the interplay between transcription factors (TFs) and their regulatory ligands (TF-RLs), remain poorly characterized and lack dedicated resources. In this context, we introduce the Actinobacteria Transcription Factor Database (Actinobacteria TFDB), a comprehensive repository that systematically integrates TF-centric data across 25 representative species. The current version encompasses 629 TFs, classified into 69 families, documents 11,776 TF-target relationships and 28 TF posttranslational modification sites. Uniquely, it features a dedicated collection of 54 experimentally validated TF-RL interactions. Beyond providing standardized annotations, sequence and structural features, and regulatory networks, Actinobacteria TFDB incorporates a specialized TF-RL module that enables interactive exploration and visualization of allosteric regulatory mechanisms. By consolidating multi-dimensional TF data from diverse sources, this resource empowers systems-level analyses and facilitates the rational design of regulatory strategies to activate silent biosynthetic gene clusters and optimize metabolite production. The database is publicly available at http://mingleadgene.com:9315/#/home.

Keywords

Actinobacteria / Transcription factors / Database

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Yu Fu, Zhan-Hui Xu, Yi-Fan Liang, Shi-Qi Yang, Xue-Qin Xie, Bang-Ce Ye, Di You. Actinobacteria TFDB: An integrated view of transcription factors in Actinobacteria. Engineering Microbiology, 2026, 6 (2) : 100272 DOI:10.1016/j.engmic.2026.100272

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Data availability statement

The web interface to the database is available at http://mingleadgene.com:9315/#/home.

Declaration of competing interest

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

CRediT authorship contribution statement

Yu Fu: Writing – original draft, Investigation, Funding acquisition, Formal analysis. Zhan-Hui Xu: Writing – original draft, Investigation, Formal analysis. Yi-Fan Liang: Writing – original draft, Investigation, Formal analysis. Shi-Qi Yang: Investigation, Formal analysis. Xue-Qin Xie: Investigation, Formal analysis. Bang-Ce Ye: Visualization, Validation, Supervision, Funding acquisition. Di You: Writing – original draft, Visualization, Validation, Supervision, Project administration, Methodology, Investigation, Funding acquisition.

References

[1]

S.C. Koech, M. Plechatá, W. Pathom—aree, Z. Kamenik, A. Jaisi, Strategies for actinobacteria isolation, cultivation, and metabolite production that are biologically important, ACS Omega 10 (2025) 15923-15934.

[2]

M. Ventura, C. Canchaya, A. Tauch, G. Chandra, G.F. Fitzgerald, K.F. Chater, D. van Sinderen, Genomics of Actinobacteria: tracing the evolutionary history of an ancient phylum, Microbiol. Mol. Biol. Rev. 71 (2007) 495-548.

[3]

A.—S. Azman, C.—I. Mawang, J.—E. Khairat, S. AbuBakar, Actinobacteria—A promising natural source of anti—biofilm agents, Int. Microbiol. 22 (2019) 403-409.

[4]

E.A. Barka, P. Vatsa, L. Sanchez, N. Gaveau—Vaillant, C. Jacquard, H.—P. Klenk, C. Clément, Y. Ouhdouch, G.P. van Wezel, Taxonomy, physiology, and natural products of actinobacteria, Microbiol. Mol. Biol. Rev. 80 (2016) 1-43.

[5]

X. Wang, R. Wang, Q. Kang, L. Bai, The antitumor agent Ansamitocin P—3 binds to cell division protein FtsZ in actinosynnema pretiosum, Biomolecules 10 (2020) 699.

[6]

Y. Wu, Q. Kang, L.—L. Zhang, L. Bai, Subtilisin—involved morphology engineering for improved antibiotic production in actinomycetes, Biomolecules 10 (2020) 851.

[7]

H.A. Tomm, L. Ucciferri, A.C. Ross, Advances in microbial culturing conditions to activate silent biosynthetic gene clusters for novel metabolite production, J. Ind. Microbiol. Biotechnol. 46 (2019) 1381-1400.

[8]

M.J. Bibb, Regulation of secondary metabolism in streptomycetes, Curr. Opin. Microbiol. 8 (2005) 208-215.

[9]

G.P. van Wezel, K.J. McDowall, The regulation of the secondary metabolism of streptomyces: new links and experimental advances, Nat Prod Rep 28 (2011) 1311.

[10]

J. Liu, J. Li, H. Dong, Y. Chen, Y. Wang, H. Wu, C. Li, D.T. Weaver, L. Zhang, B. Zhang, Characterization of an Lrp/AsnC family regulator SCO3361, controlling actinorhodin production and morphological development in Streptomyces coelicolor , Appl. Microbiol. Biotechnol. 101 (2017) 5773-5783.

[11]

X. Mu, R. Lei, S. Yan, Z. Deng, R. Liu, T. Liu, The LysR family transcriptional regulator ORF—L16 regulates spinosad biosynthesis in saccharopolyspora spinosa , Synth. Syst. Biotechnol. 9 (2024) 609-617.

[12]

M. Castro—Melchor, S. Charaniya, G. Karypis, E. Takano, W.—S. Hu, Genome—wide inference of regulatory networks in Streptomyces coelicolor, BMC Genom. 11 (2010) 578.

[13]

M. Madan Babu, S.A. Teichmann, Functional determinants of transcription factors in Escherichia coli: protein families and binding sites , Trends Genet. 19 (2003) 75-79.

[14]

J.L. Riechmann, J. Heard, G. Martin, L. Reuber, C.Z. Jiang, J. Keddie, L. Adam, O. Pineda, O.J. Ratcliffe, R.R. Samaha, R. Creelman, M. Pilgrim, P. Broun, J.Z. Zhang, D. Ghandehari, B.K. Sherman, G.L. Yu, Arabidopsis Transcription factors: genome—wide comparative analysis among eukaryotes, Science 290 (2000) 2105-2110.

[15]

W. Kim, N. Lee, S. Hwang, Y. Lee, J. Kim, S. Cho, B. Palsson, B.—K. Cho, Comparative genomics determines strain—dependent secondary metabolite production in streptomyces venezuelae strains, Biomolecules 10 (2020) 864.

[16]

Y. Ohnishi, H. Yamazaki, J.—y. Kato, A. Tomono, S. Horinouchi, AdpA, Central transcriptional regulator in the A—factor regulatory cascade that leads to morphological development and secondary metabolism in Streptomyces griseus, Biosci. Biotechnol. Biochem. 69 (2014) 431-439.

[17]

A. Higo, H. Hara, S. Horinouchi, Y. Ohnishi, Genome—wide distribution of AdpA, a global regulator for secondary metabolism and morphological differentiation in streptomyces, revealed the extent and complexity of the AdpA regulatory network, DNA Res. 19 (2012) 259-274.

[18]

D. Huang, Z.—H. Li, D. You, Y. Zhou, B.—C. Ye, Lysine acetylproteome analysis suggests its roles in primary and secondary metabolism in saccharopolyspora erythraea, Appl. Microbiol. Biotechnol. 99 (2014) 1399-1413.

[19]

J.F. Martín, P. Liras, S. Sánchez, Modulation of gene expression in actinobacteria by translational modification of transcriptional factors and secondary metabolite biosynthetic enzymes, Front Microbiol 12 (2021) 630694.

[20]

X.—M. Mao, S. Luo, R.—C. Zhou, F. Wang, P. Yu, N. Sun, X.—X. Chen, Y. Tang, Y.—Q. Li, Transcriptional regulation of the daptomycin gene cluster in Streptomyces roseosporus by an autoregulator, AtrA , J. Biol. Chem. 290 (2015) 7992-8001.

[21]

P. Zhang, Z. Zhao, H. Li, X.—L. Chen, Z. Deng, L. Bai, X. Pang, Production of the antibiotic FR—008/candicidin in Streptomyces sp FR—008 is co—regulated by two regulators, FscRI and FscRIV, from different transcription factor families , Microbiology—SGM 161 (2015) 539-552.

[22]

W. Shu, J. Stegmüller, M. Rodriguez—Estevez, C. Rückert—Reed, J. Kalinowski, O. Gromyko, Y. Rebets, A. Luzhetskyy, C. Wittmann, Metabolic engineering of Streptomyces explomaris for increased production of the reverse antibiotic nybomycin, Microb. Cell Fact. 24 (2025) 227.

[23]

J. Liu, Y. Chen, W. Wang, M. Ren, P. Wu, Y. Wang, C. Li, L. Zhang, H. Wu, D.T. Weaver, B. Zhang, Engineering of an Lrp family regulator SACE_Lrp improves erythromycin production in Saccharopolyspora erythraea , Metab. Eng. 39 (2017) 29-37.

[24]

P. Wu, K. Chen, B. Li, Y. Zhang, H. Wu, Y. Chen, S. Ren, S. Khan, L. Zhang, B. Zhang, Polyketide starter and extender units serve as regulatory ligands to coordinate the biosynthesis of antibiotics in actinomycetes, Mbio 12 (2021) e0229821.

[25]

B. Yang, Z. Li, J. Zhang, S. Qiu, X. Liu, Z. Liang, H. Yan, Y. Zhang, L. Liu, B. Xia, L. Bao, D. Li, S. Zhou, C. Corre, C. Zhang, Y. Lu, G.—Y. Tan, X. Xia, S. Li, L. Zhang, W. Wang, Scalable secondary metabolite production in Streptomyces using a plug—and—play system , Nat. Biotechnol. (2025) advance online publication.

[26]

Y. Zhuo, W. Zhang, D. Chen, H. Gao, J. Tao, M. Liu, Z. Gou, X. Zhou, B.—C. Ye, Q. Zhang, S. Zhang, L.—X. Zhang, Reverse biological engineering of hrdB to enhance the production of avermectins in an industrial strain of Streptomyces avermitilis, Proc. Natl. Acad. Sci. 107 (2010) 11250-11254.

[27]

Q. Chen, J. Zhu, X. Li, Y. Wen, Transcriptional regulator DasR represses daptomycin production through both direct and cascade mechanisms in streptomyces roseosporus, Antibiotics 11 (2022) 1065.

[28]

H. Yang, W. Sha, Z. Liu, T. Tang, H. Liu, L. Qin, Z. Cui, J. Chen, F. Liu, R. Zheng, X. Huang, J. Wang, Y. Feng, B. Ge, Lysine acetylation of DosR regulates the hypoxia response of mycobacterium tuberculosis, Emerg Microbes Infect 7 (2018) 1-14.

[29]

J.F. Martín, P. Liras, The balance metabolism safety net: integration of stress signals by interacting transcriptional factors in streptomyces and related actinobacteria, Front Microbiol 10 (2020) 3120.

[30]

J. Shi, Z. Feng, J. Xu, F. Li, Y. Zhang, A. Wen, F. Wang, Q. Song, L. Wang, H. Cui, S. Tong, P. Chen, Y. Zhu, G. Zhao, S. Wang, Y. Feng, W. Lin, Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria, Proc. Natl. Acad. Sci. 120 (2023) e2300282120.

[31]

A. Tabib—Salazar, B. Liu, P. Doughty, R.A. Lewis, S. Ghosh, M.—L. Parsy, P.J. Simpson, K. O’Dwyer, S.J. Matthews, M.S. Paget, The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase, Nucleic Acids Res. 41 (2013) 5679-5691.

[32]

N. Rabhi, S.A. Hannou, P. Froguel, J.—S. Annicotte, Cofactors As metabolic sensors driving cell adaptation in physiology and disease, Front. Endocrinol. 8 (2017) 304.

[33]

C. Bei, J. Zhu, P.H. Culviner, M. Gan, E.J. Rubin, S.M. Fortune, Q. Gao, Q. Liu, Genetically encoded transcriptional plasticity underlies stress adaptation in Mycobacterium tuberculosis, Nat. Commun. 15 (2024) 3088.

[34]

J.—h. Wu, X.—w. Chen, Y.—l. Liu, J.—y. Wu, Z.—g. Chen, B. Peng, Metabolism—dependent succinylation governs resource allocation for antibiotic resistance, Sci. Adv. 11 (2025) eadu2856.

[35]

Y.—T. Chen, G.K. Lohia, S. Chen, S.A. Riquelme, Immunometabolic regulation of bacterial infection, biofilms, and antibiotic susceptibility, J. Innate Immun. 16 (2024) 143-158.

[36]

C. Auriol, G. Bestel—Corre, J.—B. Claude, P. Soucaille, I. Meynial—Salles, Stress—induced evolution of Escherichia coli points to original concepts in respiratory cofactor selectivity , Proc. Natl. Acad. Sci. 108 (2011) 1278-1283.

[37]

H. Satam, K. Joshi, U. Mangrolia, S. Waghoo, G. Zaidi, S. Rawool, R.P. Thakare, S. Banday, A.K. Mishra, G. Das, S.K. Malonia, Next—generation sequencing technology: current trends and advancements, Biology 12 (2023) 997.

[38]

R. Seshadri, S. Roux, K.J. Huber, D. Wu, S. Yu, D. Udwary, L. Call, S. Nayfach, R.L. Hahnke, R. Pukall, J.R. White, N.J. Varghese, C. Webb, K. Palaniappan, L.C. Reimer, J. Sardà, J. Bertsch, S. Mukherjee, T.B.K. Reddy, P.P. Hajek, M. Huntemann, I.M.A. Chen, A. Spunde, A. Clum, N. Shapiro, Z.—Y. Wu, Z. Zhao, Y. Zhou, L. Evtushenko, S. Thijs, V. Stevens, E.A. Eloe—Fadrosh, N.J. Mouncey, Y. Yoshikuni, W.B. Whitman, H.—P. Klenk, T. Woyke, M. Göker, N.C. Kyrpides, N.N. Ivanova, Expanding the genomic encyclopedia of actinobacteria with 824 isolate reference genomes, Cell Genomics 2 (2022) 100213.

[39]

J.E. Galagan, K. Minch, M. Peterson, A. Lyubetskaya, E. Azizi, L. Sweet, A. Gomes, T. Rustad, G. Dolganov, I. Glotova, T. Abeel, C. Mahwinney, A.D. Kennedy, R. Allard, W. Brabant, A. Krueger, S. Jaini, B. Honda, W.—H. Yu, M.J. Hickey, J. Zucker, C. Garay, B. Weiner, P. Sisk, C. Stolte, J.K. Winkler, Y. Van de Peer, P. Iazzetti, D. Camacho, J. Dreyfuss, Y. Liu, A. Dorhoi, H.—J. Mollenkopf, P. Drogaris, J. Lamontagne, Y. Zhou, J. Piquenot, S.T. Park, S. Raman, S.H.E. Kaufmann, R.P. Mohney, D. Chelsky, D.B. Moody, D.R. Sherman, G.K. Schoolnik, The mycobacterium tuberculosis regulatory network and hypoxia, Nature 499 (2013) 178-183.

[40]

Y.—H. Yang, E. Song, J.—N. Kim, B.—R. Lee, E.—J. Kim, S.—H. Park, W.—S. Kim, H.—Y. Park, J.—M. Jeon, T. Rajesh, Y.—G. Kim, B.—G. Kim, Characterization of a new ScbR—like γ—butyrolactone binding regulator (SlbR) in Streptomyces coelicolor, Appl. Microbiol. Biotechnol. 96 (2012) 113-121.

[41]

E.W. Sayers, E.E. Bolton, J.R. Brister, K. Canese, J. Chan, Donald C. Comeau, R. Connor, K. Funk, C. Kelly, S. Kim, T. Madej, A. Marchler—Bauer, C. Lanczycki, S. Lathrop, Z. Lu, F. Thibaud—Nissen, T. Murphy, L. Phan, Y. Skripchenko, T. Tse, J. Wang, R. Williams, Barton W. Trawick, Kim D. Pruitt, Stephen T. Sherry, Database resources of the national center for biotechnology information, Nucleic Acids Res. 50 (2022) D20-D26.

[42]

M. Kanehisa, M. Furumichi, Y. Sato, M. Kawashima, M. Ishiguro—Watanabe, KEGG for taxonomy—based analysis of pathways and genomes, Nucleic Acids Res. 51 (2023) D587-D592.

[43]

S. Kim, J. Chen, T. Cheng, A. Gindulyte, J. He, S. He, Q. Li, B.A. Shoemaker, P.A. Thiessen, B. Yu, L. Zaslavsky, J. Zhang, E.E. Bolton, PubChem in 2021: new data content and improved web interfaces, Nucleic Acids Res. 49 (2021) D1388-D1395.

[44]

UniProt: the Universal protein knowledgebase in 2025, Nucleic Acids Res. 53 (2025) D609-D617.

[45]

A. Zorro—Aranda, J.M. Escorcia—Rodríguez, J.K. González—Kise, J.A. Freyre—González, Curation, inference, and assessment of a globally reconstructed gene regulatory network for Streptomyces coelicolor, Sci. Rep. 12 (2022) 2840.

[46]

N. Tschowri, Maria A. Schumacher, S. Schlimpert, Naga b. Chinnam, Kim C. Findlay, Richard G. Brennan, Mark J. Buttner, Tetrameric c—di—GMP mediates effective transcription factor dimerization to control streptomyces development, Cell 158 (2014) 1136-1147.

[47]

Y. Xu, Y. Tang, N. Wang, J. Liu, X. Cai, H. Cai, J. Li, G. Tan, R. Liu, L. Bai, L. Zhang, H. Wu, B. Zhang, Transcriptional regulation of a leucine—responsive regulatory protein for directly controlling lincomycin biosynthesis in Streptomyces lincolnensis, Appl. Microbiol. Biotechnol. 104 (2020) 2575-2587.

[48]

W. Liu, Q. Zhang, J. Guo, Z. Chen, J. Li, Y. Wen, M.A. Elliot, Increasing avermectin production in streptomyces avermitilis by manipulating the expression of a novel TetR—Family regulator and its target gene product, Appl. Environ. Microbiol. 81 (2015) 5157-5173.

[49]

C. Zhu, Y. Liu, L. Hu, M. Yang, Z.G. He, Molecular mechanism of the synergistic activity of ethambutol and isoniazid against mycobacterium tuberculosis, J Biol Chem 293 (2018) 16741-16750.

[50]

X. Ling, X. Liu, K. Wang, M. Guo, Y. Ou, D. Li, Y. Xiang, J. Zheng, L. Hu, H. Zhang, W. Li, Lsr2 acts as a cyclic di—GMP receptor that promotes keto—mycolic acid synthesis and biofilm formation in mycobacteria, Nat. Commun. 15 (2024) 695.

[51]

K. Wang, X. Cui, X. Ling, J. Chen, J. Zheng, Y. Xiang, W. Li, d—xylose blocks the broad negative regulation of XylR on lipid metabolism and affects multiple physiological characteristics in mycobacteria, Int. J. Mol. Sci. 24 (2023).

[52]

D. You, L.C. Zhao, Y. Fu, Z.Y. Peng, Z.Q. Chen, B.C. Ye, Allosteric regulation by c—di—AMP modulates a complete N—acetylglucosamine signaling cascade in saccharopolyspora erythraea, Nat. Commun. 15 (2024) 3825.

[53]

Y. Fu, Y.Q. Dong, J.L. Shen, B.C. Yin, B.C. Ye, D. You, A meet—up of acetyl phosphate and c—di—GMP modulates BldD activity for development and antibiotic production, Nucleic Acids Res. 51 (2023) 6870-6882.

[54]

D. You, B.C. Yin, Z.H. Li, Y. Zhou, W.B. Yu, P. Zuo, B.C. Ye, Sirtuin—dependent reversible lysine acetylation of glutamine synthetases reveals an autofeedback loop in nitrogen metabolism, Proc. Natl. Acad. Sci. U. S. A. 113 (2016) 6653-6658.

[55]

W. Duan, X. Li, Y. Ge, Z. Yu, P. Li, J. Li, L. Qin, J. Xie, Mycobacterium tuberculosis Rv1473 is a novel macrolides ABC efflux pump regulated by WhiB7, Future Microbiol. 14 (2019) 47-59.

[56]

J.L. Rowland, M. Niederweis, A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis, J. Bacteriol. 195 (2013) 3724-3733.

[57]

J. Haist, S.A. Neumann, M.M. Al—Bassam, S. Lindenberg, M.A. Elliot, N. Tschowri, Specialized and shared functions of diguanylate cyclases and phosphodiesterases in Streptomyces development, Mol. Microbiol. 114 (2020) 808-822.

[58]

S. Horinouchi, Y. Ohnishi, D.K. Kang, The A—factor regulatory cascade and cAMP in the regulation of physiological and morphological development in Streptomyces griseus, J. Ind. Microbiol. Biotechnol. 27 (2001) 177-182.

[59]

M. Lyu, Y. Cheng, X. Han, Y. Wen, Y. Song, J. Li, Z. Chen, AccR, a TetR family transcriptional repressor, coordinates short—chain acyl coenzyme A homeostasis in streptomyces avermitilis, Appl. Environ. Microbiol. 86 (2020) e00508—20.

[60]

J. Guo, X. Zhang, X. Lu, W. Liu, Z. Chen, J. Li, L. Deng, Y. Wen, SAV4189, a MarR—Family regulator in Streptomyces avermitilis, Activates Avermectin Biosynthesis, Front Microbiol 9 (2018) 1358.

[61]

T. Lu, X. Wu, Q. Cao, Y. Xia, L. Xun, H. Liu, Sulfane sulfur posttranslationally modifies the global regulator AdpA to influence actinorhodin production and morphological differentiation of streptomyces coelicolor, mBio 13 (2022) e0386221.

[62]

S. Honma, S. Ito, S. Yajima, Y. Sasaki, Nitric oxide signaling for aerial mycelium formation in streptomyces coelicolor A3(2) M145, Appl. Environ. Microbiol. 88 (2022) e0122222.

[63]

J.S. Hahn, S.Y. Oh, K.F. Chater, Y.H. Cho, J.H. Roe, H2O2—sensitive fur—like repressor CatR regulating the major catalase gene in Streptomyces coelicolor, J. Biol. Chem. 275 (2000) 38254-38260.

[64]

E. Palazzotto, G. Renzone, P. Fontana, L. Botta, A. Scaloni, A.M. Puglia, G. Gallo, Tryptophan promotes morphological and physiological differentiation in Streptomyces coelicolor, Appl. Microbiol. Biotechnol. 99 (2015) 10177-10189.

[65]

A. Derouaux, D. Dehareng, E. Lecocq, S. Halici, H. Nothaft, F. Giannotta, G. Moutzourelis, J. Dusart, B. Devreese, F. Titgemeyer, J. Van Beeumen, S. Rigali, Crp of Streptomyces coelicolor is the third transcription factor of the large CRP—FNR superfamily able to bind cAMP, Biochem. Biophys. Res. Commun. 325 (2004) 983-990.

[66]

H. Nothaft, S. Rigali, B. Boomsma, M. Swiatek, K.J. McDowall, G.P. van Wezel, F. Titgemeyer, The permease gene nagE2 is the key to N—acetylglucosamine sensing and utilization in Streptomyces coelicolor and is subject to multi—level control, Mol. Microbiol. 75 (2010) 1133-1144.

[67]

L. Li, W. Jiang, Y. Lu, A novel two—component system, GluR—GluK, involved in glutamate sensing and uptake in streptomyces coelicolor, J. Bacteriol. 199 (2017) e00097—17.

[68]

M. Kotowska, M. Świat, J. Zaręba—Pasławska, P. Jaworski, K. Pawlik, A GntR—like transcription factor HypR regulates expression of genes associated with l—hydroxyproline utilization in streptomyces coelicolor A3(2), Front. Microbiol. 10 (2019) 1451.

[69]

H.M. Kim, B.E. Ahn, J.H. Lee, J.H. Roe, Regulation of a nickel—cobalt efflux system and nickel homeostasis in a soil actinobacterium streptomyces coelicolor, Metallomics 7 (2015) 702-709.

[70]

A. Volbeda, E.L. Dodd, C. Darnault, J.C. Crack, O. Renoux, M.I. Hutchings, N.E. Le Brun, J.C. Fontecilla—Camps, Crystal structures of the NO sensor NsrR reveal how its iron—sulfur cluster modulates DNA binding, Nat. Commun. 8 (2017) 15052.

[71]

J.S. Hahn, S.Y. Oh, J.H. Roe, Role of OxyR as a peroxide—sensing positive regulator in Streptomyces coelicolor A3(2), J. Bacteriol. 184 (2002) 5214-5222.

[72]

E. Takano, R. Chakraburtty, T. Nihira, Y. Yamada, M.J. Bibb, A complex role for the gamma—butyrolactone SCB1 in regulating antibiotic production in Streptomyces coelicolor A3(2), Mol. Microbiol. 41 (2001) 1015-1028.

[73]

W. Wang, J. Ji, X. Li, J. Wang, S. Li, G. Pan, K. Fan, K. Yang, Angucyclines as signals modulate the behaviors of Streptomyces coelicolor, Proc. Natl. Acad. Sci. U. S. A. 111 (2014) 5688-5693.

[74]

G. Xu, J. Wang, L. Wang, X. Tian, H. Yang, K. Fan, K. Yang, H. Tan, Pseudo" gamma—butyrolactone receptors respond to antibiotic signals to coordinate antibiotic biosynthesis, J. Biol. Chem. 285 (2010) 27440-27448.

[75]

K.L. Lee, J.S. Yoo, G.S. Oh, A.K. Singh, J.H. Roe, Simultaneous activation of iron— and thiol—based sensor—regulator systems by redox—active compounds, Front. Microbiol. 8 (2017) 139.

[76]

H. Huang, A. Grove, The transcriptional regulator TamR from Streptomyces coelicolor controls a key step in central metabolism during oxidative stress, Mol. Microbiol. 87 (2013) 1151-1166.

[77]

H. Huang, S. Sivapragasam, A. Grove, The regulatory role of Streptomyces coelicolor TamR in central metabolism, Biochem. J. 466 (2015) 347-358.

[78]

S. Sivapragasam, A. Grove, Streptomyces coelicolor XdhR is a direct target of ppGpp that controls expression of genes encoding xanthine dehydrogenase to promote purine salvage, Mol. Microbiol. 100 (2016) 701-718.

[79]

X.M. Mao, Z.H. Sun, B.R. Liang, Z.B. Wang, W.H. Feng, F.L. Huang, Y.Q. Li, Positive feedback regulation of stgR expression for secondary metabolism in Streptomyces coelicolor, J. Bacteriol. 195 (2013) 2072-2078.

[80]

I. Yevshin, R. Sharipov, S. Kolmykov, Y. Kondrakhin, F. Kolpakov, GTRD: a database on gene transcription regulation—2019 update, Nucleic Acids Res. 47 (2019) D100-D105.

[81]

C. Feng, C. Song, Y. Liu, F. Qian, Y. Gao, Z. Ning, Q. Wang, Y. Jiang, Y. Li, M. Li, J. Chen, J. Zhang, C. Li, KnockTF: a comprehensive human gene expression profile database with knockdown/knockout of transcription factors, Nucleic Acids Res. 48 (2020) D93-D100.

[82]

S. Mukherjee, S. Das Mandal, N. Gupta, M. Drory—Retwitzer, D. Barash, S. Sengupta, RiboD: a comprehensive database for prokaryotic riboswitches, Bioinformatics 35 (2019) 3541-3543.

[83]

R. Penchovsky, N. Pavlova, D. Kaloudas, RSwitch: a novel bioinformatics database on riboswitches as antibacterial drug targets, IEEE/ACM Trans. Comput. Biol. Bioinform. 18 (2021) 804-808.

[84]

S. Kiliç, E.R. White, D.M. Sagitova, J.P. Cornish, I. Erill, CollecTF: a database of experimentally validated transcription factor—binding sites in bacteria, Nucleic Acids Res. 42 (2014) D156-D160.

[85]

H.E. Augustijn, D. Karapliafis, K.M.M. Joosten, S. Rigali, G.P. van Wezel, M.H. Medema, LogoMotif: a comprehensive database of transcription factor binding site profiles in actinobacteria, J. Mol. Biol. 436 (2024) 168558.

[86]

P.S. Novichkov, A.E. Kazakov, D.A. Ravcheev, S.A. Leyn, G.Y. Kovaleva, R.A. Sutormin, M.D. Kazanov, W. Riehl, A.P. Arkin, I. Dubchak, D.A. Rodionov, RegPrecise 3.0—a resource for genome—scale exploration of transcriptional regulation in bacteria, BMC Genom. 14 (2013) 745.

[87]

M. Ryndak, S. Wang, I. Smith, PhoP, a key player in mycobacterium tuberculosis virulence, Trends Microbiol. 16 (2008) 528-534.

[88]

H. Yan, X. Lu, D. Sun, S. Zhuang, Q. Chen, Z. Chen, J. Li, Y. Wen, BldD, a master developmental repressor, activates antibiotic production in two Streptomyces species, Mol. Microbiol. 113 (2020) 123-142.

[89]

H.U. van der Heul, B.L. Bilyk, K.J. McDowall, R.F. Seipke, G.P. van Wezel, Regulation of antibiotic production in actinobacteria: new perspectives from the post—genomic era, Nat. Prod. Rep. 35 (2018) 575-604.

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