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Database: UniProt
Entry: A0A1Q5CD88_9ACTN
LinkDB: A0A1Q5CD88_9ACTN
Original site: A0A1Q5CD88_9ACTN 
ID   A0A1Q5CD88_9ACTN        Unreviewed;       352 AA.
AC   A0A1Q5CD88;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=OmpR/PhoB-type domain-containing protein {ECO:0000259|PROSITE:PS51755};
GN   ORFNames=A6A27_15740 {ECO:0000313|EMBL:OKI81560.1};
OS   Micromonospora sp. CB01531.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI81560.1, ECO:0000313|Proteomes:UP000186700};
RN   [1] {ECO:0000313|EMBL:OKI81560.1, ECO:0000313|Proteomes:UP000186700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01531 {ECO:0000313|EMBL:OKI81560.1,
RC   ECO:0000313|Proteomes:UP000186700};
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:OKI81560.1}.
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DR   EMBL; LWLS01000024; OKI81560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5CD88; -.
DR   STRING; 1718947.A6A27_15740; -.
DR   OrthoDB; 3208838at2; -.
DR   Proteomes; UP000186700; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15831; BTAD; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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; PF00486; Trans_reg_C; 1.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
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:UP000186700}.
FT   DOMAIN          1..92
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        1..92
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          288..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  38868 MW;  C191E58311F5AB15 CRC64;
     MRFRLLGPLT VGSEDSPLDI RGNRLRAVLA LLLINSGAVV PMDDIIKAVW GETPPRTVRT
     QVQVQISTLR ALFQSIEGVK ISTHPAGYSL HAPPGEIDVL VFDQLVQRGR ALSAGRQLDA
     AAALFREALE LYHGPPLCNV DAPFAQLAGV RLQERRLDVL GELFGLELRL GRHQEIVPTL
     TELVAEHPLR ETFWRHLVVA LHGAGRRGEA IATYHQVRRL LREELGLDPG RELVAAYRDL
     LEEEPTAPST VDREALAATL DCLRLTEQLL RDLRRQLEAL SLSLAGPADG CRGPESRAHD
     SMTAVADEDQ TTSQSTVMEW VEPSRSRTEK SCGPEQFRLA RVLTSIRPVV GL
//
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