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Database: UniProt
Entry: A0A1C5F5R8_9ACTN
LinkDB: A0A1C5F5R8_9ACTN
Original site: A0A1C5F5R8_9ACTN 
ID   A0A1C5F5R8_9ACTN        Unreviewed;       948 AA.
AC   A0A1C5F5R8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=DNA-binding transcriptional activator of the SARP family {ECO:0000313|EMBL:SCG02909.1};
GN   ORFNames=GA0115259_108032 {ECO:0000313|EMBL:SCG02909.1};
OS   Streptomyces sp. MnatMP-M17.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCG02909.1, ECO:0000313|Proteomes:UP000198886};
RN   [1] {ECO:0000313|EMBL:SCG02909.1, ECO:0000313|Proteomes:UP000198886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCG02909.1,
RC   ECO:0000313|Proteomes:UP000198886};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
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DR   EMBL; FMDK01000757; SCG02909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5F5R8; -.
DR   Proteomes; UP000198886; Unassembled WGS sequence.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15831; BTAD; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR005158; BTAD.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR35807:SF1; TRANSCRIPTIONAL REGULATOR REDD; 1.
DR   PANTHER; PTHR35807; TRANSCRIPTIONAL REGULATOR REDD-RELATED; 1.
DR   Pfam; PF03704; BTAD; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00028; TPR; 4.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Reference proteome {ECO:0000313|Proteomes:UP000198886};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..97
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   REPEAT          853..886
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DNA_BIND        1..97
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          245..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  103237 MW;  60BDBF8FFDD37F64 CRC64;
     MGLPVEFGLL GSIEARLDGR PVELGHARQR CVLAALMADA NRLVSVDQLI DRVWGERPPQ
     RAQASLYSYI SRLRQALSPA AGDADIERRS GGYVLTVDTS AVDLHRFREL VERARTADDS
     EAEALFEEAL ALWRGDAATE QDSPWFNSLR EALRRERHAA ELDLVDIRLR SGRHTGLPAE
     LATRVEAHPL DERLVGQLML ALYRGGRPAD ALARYEEIRQ RLATELGTDP GPPLRELRQR
     ILTADPVLDK PAPVRRTPGS SGSPVEPAAP PAPVPRQLPA PPPMFTGRSR ELARLGKLLE
     PRAERGGTVV ISAIGGTGGI GKTWLALRWA HSRQERFPDG QLYADLRGFS PSGEPVPAAV
     VVRAFLEALG APPGTIPADP DAQAALYRSL TAGKRLLILL DNARSTTQVL PLLPGSPTCT
     VLVTSRHQLT GLTAAHGGTP LTLDVLTDTE ALELLTRHLG AARIAAEPDA AATLLKHCAG
     LPLAISILAA RATMNPALSL AALASELHEA ATRLDALDAG ETATDLRAVF ASSYEALDAP
     TARVFRLLSL APGADIGLPA AASLTGLPLS RLRAHLRTLH SAHLVQEHTP HRYTCHDLLR
     AYATELAQSF DTEAERTAAL DRLLDHYVHT AFAADRLLLP HRDPLTLPPP ADGLTPERLA
     DHDEAMKWFS REHTVLTAAV EHAARLGLDA RVWQLAWATL TFQSRLGHWH EVESAQRAAL
     AAAVRLGDRS AQAECRRGLA WALSQTARVD EARDELEVAL ALSRDLGDDP GRAHAHLTLS
     WLCELEGDER AAYEHDLTAL DLFTSSSHRS GRARALNALG WDRIQRGDYQ QAVLDCEEAL
     ALQQELDDER GQAGTWDTLG YAYQRIGDHG NAKECFRHSL RLNRALGHRF NEAETLIHLG
     ETHRATGALP AAREAWQQAL TVLIGIGHPE TELDRVRTML QELNTPTN
//
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