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Database: UniProt
Entry: K4R9P8_STRDJ
LinkDB: K4R9P8_STRDJ
Original site: K4R9P8_STRDJ 
ID   K4R9P8_STRDJ            Unreviewed;       984 AA.
AC   K4R9P8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Regulatory protein AfsR {ECO:0000313|EMBL:CCK29394.1};
GN   Name=afsR {ECO:0000313|EMBL:CCK29394.1};
GN   ORFNames=BN159_5015 {ECO:0000313|EMBL:CCK29394.1};
OS   Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK29394.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK29394.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC   {ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA   Pelzer S., Kalinowski J., Mack M.;
RT   "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT   heterologous production of the unique antibiotic roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
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DR   EMBL; HE971709; CCK29394.1; -; Genomic_DNA.
DR   RefSeq; WP_015659734.1; NC_020504.1.
DR   AlphaFoldDB; K4R9P8; -.
DR   STRING; 1214101.BN159_5015; -.
DR   KEGG; sdv:BN159_5015; -.
DR   PATRIC; fig|1214101.3.peg.5084; -.
DR   eggNOG; COG3629; Bacteria.
DR   eggNOG; COG3903; Bacteria.
DR   HOGENOM; CLU_004665_2_0_11; -.
DR   OrthoDB; 3845029at2; -.
DR   Proteomes; UP000008043; Chromosome.
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   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:UP000008043};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          16..112
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   REPEAT          854..887
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DNA_BIND        16..112
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   984 AA;  105687 MW;  08A045667D90973A CRC64;
     MDGVPRVPEQ RRGGRDGSTE PTALRFSVLG PVRAWRGEEA LNTGSPQQRA LLAALLLREG
     RTATAAELID ALWGEEPPSQ ALAALRTYAS RLRKVLDPGV LASESGGYAV RSLGEGALDL
     SVAQELATEA EKARGTGDLC HARDVLNRVL SLWDGEALAG VPGPYAEAQR VRLEEWRLQL
     LESRLDMDLE QGCHAEAVSE LTALTAAHPL RERLRELLML ALYRSGRQAE ALAVYADTRR
     LLADELGVDP RPGLRELQQR ILQADPGLAE PSAPLAEPAV VPVRPAQLPA TVPDFTGRSS
     FVTELSDVLA SAEGRVMAVS ALAGIGGVGK TTLAVHVAHQ ARSAFPDGQL YVDLQGAGSR
     AADPETVLGS FLRALGTADS AIPDSLEERA ALYRSVLDGR RVLVLLDNAR DAAQVRPLLP
     GTSGCAALVT SRVRMVDLAG AHLVDLDVMS PDEALSLFTK IVGEERVASE REAALDVVAA
     CGFLPLAIRI AASRLAARRT WTVSVLAAKL GDERRRLDEL QAGDLAVKAT IELGYGQLEP
     AQARAFRLLG LADGPDISLA AAAALLDLGV EETEELLESL VDTSLLESAA PGRYRFHDLV
     RLYARACAER DEWPPSERGA ALSRLLDFYL ATTAQVYAIE HGEDRLIDHL EPTRYPGLRF
     TEAPTALDWL YTEAGQLLAC VRQAAGTERL RRAVDLLWAA KDLTESGANS HQYEMTAKAT
     CEATRVAGHE RAEGRARTVL SDVLLVSGRV REAEQEARVA MELAASARDS IAVSWVANNR
     GLICLHESRF ADGKVFFDQA LEGLRATGNR PFEATVLGNL SRAHLGLGNI AKAVEIAQSG
     LAVHTEVGRT VRLANGHFQL GVALTRAGRY TEALSQFSDA LGLFNDHRQR LWEGVTHFRT
     AEVHAAEHRA AHAAQHAEQA LALGCIGGDR MRGNVLTLLG RSLSALGQAD RARACWREAL
     NLYEQNSAPE AEEARALLTS AAAA
//
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