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Database: UniProt
Entry: A0A291QA76_9ACTN
LinkDB: A0A291QA76_9ACTN
Original site: A0A291QA76_9ACTN 
ID   A0A291QA76_9ACTN        Unreviewed;       992 AA.
AC   A0A291QA76;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=OmpR/PhoB-type domain-containing protein {ECO:0000259|PROSITE:PS51755};
GN   ORFNames=KY5_3514 {ECO:0000313|EMBL:ATL28532.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL28532.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL28532.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL28532.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) 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; CP022685; ATL28532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291QA76; -.
DR   KEGG; sfk:KY5_3514; -.
DR   Proteomes; UP000221011; 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:UP000221011};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          25..121
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   REPEAT          862..895
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DNA_BIND        25..121
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  106709 MW;  BD07F6E11020AA5C CRC64;
     MVDVPRVPEQ WRPASGNTPE ERTEGEFPEV QASRFSVLGP VRAWHGTEQL NTGSPMQRAL
     LAALLLRDGR TATASELIDA LWGDEPPSQA LAAVRTYASR LRKVLPPGVL LSESGGYAVR
     VTEGALDLTA AEDLWAAAEK ARGVGDLCQA RSLVNKALGL WDGEPLANVP GPYAETQRTR
     LEEWRLQIVE SRLDMDLEQG CHAEAVSELT ALTAAHPLRE RLRELLMLAL YRSGRQAEAL
     AVYADTRRLL ADELGVDPRT GLKELQQRIL QADPALSEPS AGDPEPATTV VRPAQLPATV
     PDFTGRKSFV DELSDILSTA EGRVMAVSAL AGIGGVGKTT LAVHVAHVAR THFPDGQLYV
     DLQGAGARAA EPETVLGAFL RALGTADSAI PESLEERAAL YRSVLDGRRV LVLLDNARDA
     AQVRPLLPGM EGCAALVTSR VRMVDLAGAH LVDLDVMSPE EALLLFTRIV GDERVTSERE
     AALDVVAACG FLPLAIRIAA SRLAARRTWT VSTLAAKLAD ERRRLDELQA GDLAVKATFE
     LGYGQLEPAQ ARAFRLLGLA DGPDLSLAAA AAVLDLPLED TEDLLEALVD TSLIESAAPG
     RYRYHDLVRL YARACAERDE QPPSERDAAM SRLLDFYLAS AARVYAIERP GDRTVSHLEV
     THHLGLEFDD AATAFSWLRA EAACILACVQ QSLAPNSLRR AVDLILAAKN LAESGASSHR
     YEAVTRAARD VAAATGDAYA EGRARVSLAQ VLNKLGRFHD AYAELELAVQ LALESGDPWT
     HGNALNEQGI VNNCINQPAV GEGQLLQAIS AFRADGNRHS EASALCNLSR ALLAMGRTNK
     SIELAQQGMA IYSELGVTFR LANAKYALGL ALSQAGRHSE ALDQLTDALE IFRDSRQRLW
     QGTTHYRIAQ VSFSDRRVTQ AAQHAEQALS TGCVGGDWMR ANVLTILGRA LRALGQVDRA
     QACWSEALAI HEAGGAPEAA QLRELLKPVA AA
//
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