ID Q846X0_STRCM Unreviewed; 980 AA. AC Q846X0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 06-FEB-2007, entry version 27. DE Putative regulatory protein. GN Name=monH; OS Streptomyces cinnamonensis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1900; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC15413; RX MEDLINE=22823264; PubMed=12940979; RX DOI=10.1046/j.1365-2958.2003.03571.x; RA Oliynyk M., Stark C.B., Bhatt A., Jones M.A., Hughes-Thomas Z.A., RA Wilkinson C., Oliynyk Z., Demydchuk Y., Staunton J., Leadlay P.F.; RT "Analysis of the biosynthetic gene cluster for the polyether RT antibiotic monensin in Streptomyces cinnamonensis and evidence for the RT role of monB and monC genes in oxidative cyclization."; RL Mol. Microbiol. 49:1179-1190(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC15413; RA Oliynyk M.; RT "The gene cluster for monensin biosynthesis."; RL Thesis (1999), University of Cambridge. CC -!- FUNCTION: Positively regulates the transcription of the maltose CC regulon whose gene products are responsible for uptake and CC catabolism of malto-oligosaccharides. Binds and recognizes a DNA CC motif (called the malT box): 5'-GGA[TG]GA-3' (By similarity). CC -!- SUBUNIT: Monomer in solution but oligomerizes to an active state CC in the presence of the positive effectors ATP and maltotriose (By CC similarity). CC -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain. 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; AF440781; AAO65802.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. DR InterPro; IPR003593; AAA+_ATPase_core. DR InterPro; IPR000792; HTH_LuxR. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR011717; TPR_4. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF00196; GerE; 1. DR Pfam; PF07721; TPR_4; 1. DR PRINTS; PR00038; HTHLUXR. DR ProDom; PD000307; HTH_LuxR; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00421; HTH_LUXR; 1. DR PROSITE; PS00622; HTH_LUXR_1; 1. DR PROSITE; PS50043; HTH_LUXR_2; 1. KW ATP-binding; Carbohydrate metabolism; DNA-binding; Nucleotide-binding; KW Transcription; Transcription regulation. SQ SEQUENCE 980 AA; 102699 MW; 5070C3E097FFC735 CRC64; MSGVERGVGS AGPVEQGDGL AGLVERAEAL AALRGAFDGS PGTGGSLVVL SGAVGTGKTA LLRAWADRIG ADADALVLTA TACRAERDLP LGVLEQLVRS PGLPPASAER ALAWWDEEAS ATPGKTDANG TSANGTDANG TGAGQTGAGQ AGVGQTGVGG EPVLAASALR GLCEVLRDLL AERPVVVAVD DAHHADAASL QCLLSVVRRL RSARLHVLFT EYAHQKAQNA LLSSEFLHEP ALRRIRLEPL SKAGVEALLA RHLDERTAQD LTPVVHGMSA GHPLLVRALA EDHRAAGGAG EAYGRAVLSF LYRHETPVTQ VARAIAALGA HAGPGQVGRL LDVDAASVER AVRQLTVAEV LHEGRLCHPA FAAAVLDGMP PEERRALHGR VADLLHEEGA PATEVAAHLV AADRSDAPWA VPVFQEAAQL ALDEDQVETG VDYLRAAHQR CRGAAQRAAV VGALADAEWR LDPAKVLRHL PDPAAMAPQT DPAALAPHTD PAPTAAPTAA PTPTPIPTTP PLPTHLLWHG RVEEGLDAIG TLTGPGPNPA GAPPMNPADL DTPWLWGAYL YPGHVKERLG SGALSPQRST PPAVTPELQG AGTLMNDLLH GGERDATEAA ERALNRYRLG PRTIAVQTAA LAALTYRDRP HRAAAWCDGL VAQADERNSP TWRALFTAWR ALLHLRQGDP AAAEQRAETA LALLGSKGWG AAIGLPLAAA VQAKAALGDV DGAAALLERP VPQAVFQTRT GLHYLAARGR YHLATGCHYA ALCDFYACGT RMSSWGVDLP ALEPWRLGAA EAYLALGEGL LARQLVDGQL PLPTPDDGRT WGMTLRLRAA TSPAPARAEL LDEAVAVLRE SGDTFELARA VADQAVAVRE GGEAERARLL ARKAELLARR WGSAPAPATV PEPPERPGPA TPDAELTSAE RRVAELAAEG FTNREISRKL CVTVSTVEQH LTRIYRKLDV RRLDLQAALG //