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Database: UniProt
Entry: A0A345HS75_9ACTN
LinkDB: A0A345HS75_9ACTN
Original site: A0A345HS75_9ACTN 
ID   A0A345HS75_9ACTN        Unreviewed;      1042 AA.
AC   A0A345HS75;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=AfsR family transcriptional regulator {ECO:0000313|EMBL:AXG79549.1};
GN   ORFNames=DVK44_19970 {ECO:0000313|EMBL:AXG79549.1};
OS   Streptomyces paludis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG79549.1, ECO:0000313|Proteomes:UP000253868};
RN   [1] {ECO:0000313|Proteomes:UP000253868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA   Zhao J.;
RL   Submitted (JUL-2018) 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; CP031194; AXG79549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345HS75; -.
DR   KEGG; spad:DVK44_19970; -.
DR   OrthoDB; 3845029at2; -.
DR   Proteomes; UP000253868; 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; 3.
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; 5.
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.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Reference proteome {ECO:0000313|Proteomes:UP000253868};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          74..170
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        74..170
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  111503 MW;  747829398FFFA212 CRC64;
     MERDGEPRVP EQRERRAPVG TEGTKGGRAG DGASEDAGVR ASKNAGADAT AQGDANGNAS
     AGTSAHTNAG PGATAHPSTD ALRFSVLGPV RAWRGAETLP SGSPQQRALL AALLLREGRT
     ATAPELIDAL WGDRPPSQAL AAVRTYASRL RKVLSSGVLV SESGGYALRT GPEALDLSVA
     EELAGHADKE RAAGNRAQAR DLLNRSLELW TGEPLAAVPG PYAQTQRARL EEWRLQLTEA
     RIDMDLEAGC HAGAVSELTA LTAEHPLRER LRELLMLALY RGGRQAEALA VYADTRRLLA
     DELGVDPRPE LARLHQRILE ADALLVGPAE EPATSPAVLR PAQLPATVPD FTGRAAFVQE
     LGDRLATPEG AVMAVSAIAG IGGVGKTTLA IHVAHAARAH FPDGQLYVDL QGAGPRAAEP
     ETVLASFLRA LGMSAAAIPD SLEDRSALYR STLDGRRVLV LLDNARDAAQ VRPLLPGTDG
     CAAVVTSRGR MVDLAGAHLV DLDVMSPDEA LQLFTRIIGH ERVSSEREAA LDVVAACGFL
     PLAIRIAASR IASRRTWTVS VLAEKLADER RRLDELQAGD LAVKATFELG YGALEQSQAR
     AFRLLGLADG PDISLAAAAA LLDLPVRQAE ELLESLVDTS LLESAAPGRY RYHDLVRLYA
     RACAERDEQP ASRREDALSR LLDFYLATTA NVYALERPGD RLPDRLEATA YPGLSFTDRR
     DGEDWLYAEA NSVLACAHQA ADRPGTLRRA VDLLWASLDL GESGANSKEY EEAAAALLTA
     AGASGDPWLE GRALITMSNV HHFTGRFDRA KEKAEQARAL AHHSGDLLTM AWASNHCGII
     ALYQNRYPDG ERHLTRAIAD YRADGNEAGE ASSLCNLSRV RLALGRTASA IALAQQGMEI
     YDRTGNTLRG ANARYALGMA LAQKDHLTDA TDRLTEALKT FRDSRHRLWE GMSLFRLAEV
     DLLARRPVRA ASNAEAALTI LRDIGGDWRR ANVLTTLGRA LNSIGQTGRA HVCWREALAT
     YEELGSPEAA DVRALLSSVA AA
//
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