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Database: UniProt
Entry: A0A1Q5KBS7_9ACTN
LinkDB: A0A1Q5KBS7_9ACTN
Original site: A0A1Q5KBS7_9ACTN 
ID   A0A1Q5KBS7_9ACTN        Unreviewed;      1032 AA.
AC   A0A1Q5KBS7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=OmpR/PhoB-type domain-containing protein {ECO:0000259|PROSITE:PS51755};
GN   ORFNames=AMK32_29670 {ECO:0000313|EMBL:OKJ79026.1};
OS   Streptomyces sp. CB01883.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ79026.1, ECO:0000313|Proteomes:UP000186398};
RN   [1] {ECO:0000313|EMBL:OKJ79026.1, ECO:0000313|Proteomes:UP000186398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01883 {ECO:0000313|EMBL:OKJ79026.1,
RC   ECO:0000313|Proteomes:UP000186398};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKJ79026.1}.
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DR   EMBL; LIWA01000007; OKJ79026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5KBS7; -.
DR   OrthoDB; 3860705at2; -.
DR   Proteomes; UP000186398; 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   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; 2.
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; PF13181; TPR_8; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00028; TPR; 5.
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; 2.
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:UP000186398};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..67
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        1..67
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          219..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  108253 MW;  FF2CE629CBE76F6F CRC64;
     MLAVLLLRSG RAASMAELID GVWGDEPPYS AAAMMRTYAW RLRRSLDESP TQPQVLVSVG
     DGYRLALDPG DVDAVRAEQL AGQAAGHRAA GRPAEAAARI GQALALWHGE PLAGVPGPHA
     EQQRGRLEEV RLTLLEEHFD LLIGEGSPLL AVPELGALVS AHPLRESFHA LYIRALQRAG
     RQADALAAYH RLRTQLAETL GVEPSRELRT LYQRLLADDS SSAPAGEGEA ETPGRASGFS
     AAGSGRRSAA RTPDGGEGTS AGRGGAVSPG VVGQAAALST TGLPDDAGED AQGSPAPAGA
     ATATSSAAAG GIFVGSPPVP AQLPAGTVDF TGRSPALDRL TRALATDHGD APPVVVITGM
     GGVGKSALAV RAAHGVSARF PDGQLYADMR GNRHDPTDAG VVLTSFLTAL GVAAQFVPES
     LDDRAGLLRS LLNGRRVLIL LDDVRDATQI SPLLPGAASC AVLITSRSRL WGLPTSARVD
     LAAFEADEAV SLLERVVGPA RVAEDPAAAR ELVHSCGLLP LAVRIAASRL ASRPAWGARS
     LAVRLADERR RMAELRAGDL TVASVFEMGY RQLSEAQARA FRLVAAVCDT EIGTPAASAV
     LGMDEEDAEE QLEALVDLSL LDTSGPGRYR LHDLLRVYGQ QQATQEERLS ALDRLLDFLL
     ATAAGAFQRV VPGDAVATTL SPTRSAGVRF ADVRAARDWA AAESEAAFSV VLVAARESQV
     ADVAEPSAGP RAATRAPLLR VAVDLLIALT AFGPYVQREQ LVRAAVAVAE AAEGLADHRT
     VGRARFLCGN IAVQSARLGV ARQHLRMAET HCRENGDAPI LRQILNDLGL VALLQHDHED
     AVDRLDEAVR LARELGQRSG ALVTTVNAAL ARLRCGRVEE ARRACESALA ELRAAADHQG
     VAYALSVLGL CMHELGRYDE AVARYTECLS VCRAMELHGR EAQAHYRLAD TLRALGRPAE
     AVAAAGQAVA RCADGRAERD HGHALVALGR ALADLGRNAE AAARLGEAAA VFTRLELPDA
     LHATALREEL PV
//
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