ID D7C6Z2_STRBB Unreviewed; 1512 AA.
AC D7C6Z2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Bifunctional two-component system sensor kinase/response regulator {ECO:0000313|EMBL:ADI08379.1};
GN OrderedLocusNames=SBI_05259 {ECO:0000313|EMBL:ADI08379.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI08379.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI08379.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI08379.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002047; ADI08379.1; -; Genomic_DNA.
DR STRING; 749414.SBI_05259; -.
DR KEGG; sbh:SBI_05259; -.
DR PATRIC; fig|749414.3.peg.5434; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_002345_0_0_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADI08379.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transferase {ECO:0000313|EMBL:ADI08379.1}.
FT DOMAIN 146..221
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1389..1506
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 556..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 559..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..772
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1438
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1512 AA; 155228 MW; 7369D3CE6A1E8C26 CRC64;
MSSRPSRGAA RLAAILDALP DALLLVNCNG TVVNANHIAL ETFEVPGTAL VGRGLLDLLP
SFDSNRIPGS MRRPDDQDEG GHTKPTRMIA RRTDGMQFPV EVTSANLEDG RTPYADQYSY
TGDELLMIVV RDLTGTLDTE AELARQQRQT EMILRAAAEG VVGVDTEGKV VLVNPSAAQI
LGYRASDLGG QELHPLVHHS RPDGSPLPYE ESPLTETLRS GRKYRVRGQV LWAKDGSPVP
VDLTTAPVRD GEQLVGAVMT FTDRRPEETL VAKHAEELEN LTAKHAKELK KLTARHTEEQ
EKLTAQLAKE RKELTAQLAK EREAHTERYD ALAARNAQLL AVLDQSLRGP LVELRGELGV
LADDPAGQLW PEANQILHHL AAGYTRMTTL VDNVLSYQRL DSGGEEFTRH AVSMDEVVAA
GVEGAVELIG PGRAQFAVHA PPIEAEVDAE RLAQALAHLI ADVAGVDSTG KAAAGPGGAT
GDSTIVVAAA QRGDVVRIEV RGPYAGGDPV HEPIVRGIVR RHGGVLQTHE MPGMGGHAYV
LEVPISAAAA AQADQAENAA GASERTSGRG TGAGNTGPGS GPGSAVGQGG TNGAGTGQTP
TGPTGRRARR GPAGAAAGGT NGAGTNGAGT NGAGANGAGT DGSGANGGAD GQPPARGADP
RTPSTQGAGH RGAHAGSAPA GPAAPAPDGD STTPGQSAAA EEQQPTGRRR ARRHPDEEQQ
PAVASANAQT DGQGSGAHHH PRGSGQQPGP QAGPQANPQP GPQPPAMGPV PPQGMAGQPS
TLAGRRARRA APAEAGQGRS ALALPPAAAD AAPPAGGRPG APGPGTPPAA QGGPAMPALP
AARTPEQQQN NWEQPPSGAN AGPGPLPPAQ PAAQPAGRRR ARRALAEAPG RAGADEAQPQ
PQSQPQLQPQ AQPQPAGDPV GGRSPFALPP AAADRTPQSA LPPELGPVGL VPAQHGARDP
RGNAPQAAQG GAPVPSRGGG LAVRGGPVPP NAGQPSGGWP AAPGPGTPPA AQGGPAMPAL
PAARTPEQQQ NNWEQPPSGQ AAPDGPYDTD EGPYDAYDTG EMDDAPQPTG RRRARRPLAD
EQSAPGGMPA VEEGAPQPGA WPGGPVQPQP QPLPQPQRRP QQLPAEAGPG PDASQGRAIS
VRTLGQGVPF AQQVSEQHPH HPQGQPQTPS GGTAAAGASG RRRKLAARPD PAAPATSAEL
EPAGRAQPPH PGAQPRPQQG PGPGRPGSPQ TAGRAFAIGA PDEGAEGPEP LDGPNGAIEI
VDDRTPPPDD ELPPEPLDNP RRLLVWPAPD MSTQQALSDR GYRPVIVHSR EEVDAQIAAY
PAALFVDPLT GPITRTALQS LRTAAVAAEV PVLVTAGLGQ ASREAAYGAD PAVLFKALAP
RDSEQHPPRV LLIEEHQPIS EALTATLERR GMQVARAATD ADAVALAAQM RPNLVVMDLM
QVRRRRAGIV DWLRGNGLLN RTPLVVYTSA DIDPANLSRL SSGETVLFLA ERSTSTEVQG
RIVDLLAKIG NN
//