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Database: UniProt
Entry: C1B6E6_RHOOB
LinkDB: C1B6E6_RHOOB
Original site: C1B6E6_RHOOB 
ID   C1B6E6_RHOOB            Unreviewed;      1087 AA.
AC   C1B6E6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:BAH51249.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:BAH51249.1};
GN   OrderedLocusNames=ROP_30020 {ECO:0000313|EMBL:BAH51249.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH51249.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH51249.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH51249.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AP011115; BAH51249.1; -; Genomic_DNA.
DR   RefSeq; WP_012690205.1; NC_012522.1.
DR   AlphaFoldDB; C1B6E6; -.
DR   STRING; 632772.ROP_30020; -.
DR   KEGG; rop:ROP_30020; -.
DR   PATRIC; fig|632772.20.peg.3137; -.
DR   HOGENOM; CLU_004665_5_3_11; -.
DR   OrthoDB; 136365at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47691:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR RV0890C-RELATED; 1.
DR   PANTHER; PTHR47691; REGULATOR-RELATED; 1.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00220; S_TKc; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Kinase {ECO:0000313|EMBL:BAH51249.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAH51249.1};
KW   Transferase {ECO:0000313|EMBL:BAH51249.1}.
FT   DOMAIN          26..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1018..1083
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50043"
FT   REGION          309..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1087 AA;  117144 MW;  9C14214831AECA13 CRC64;
     MTDVDPFATQ RDVSGSVTAE LAVAGFEDAQ EIGRGGFGIV YRCTQIALDR TVAVKVLTAD
     LDEENRARFL REQRAAGRLT GHPNIVNVLH AGVTENGRPF IVMPYQAQGS LDERIRRHGP
     LPLDEALRLG VKMAGALETA HRLGILHRDV KPGNILITDY GEPALTDFGI AHIAGGFETS
     EGIVTGSPAF TAPEVVAGDP PTPAADVYGL GAALFAALTG HAAFERRSGE QLVAQFLRIA
     SEPVPNPREH GVPEDVSAVV ERAMSSEPGA RPSAVELGRQ LREAQLHHGF PVDEMAMHAE
     PIAVQSGSSA VGQGAQGRPG WSPADSGRTG GLPLELTSFV DRRTELAEAT NLLSTSRLVT
     LTGIGGVGKT RLAIRAATKV QRNFADGVTL VELGELRDDS LLPGVVAAAL GVRDQSARSA
     HDVLVEYLAP RDLLLVLDNC EQVVAAAAKL AEILLRACPQ VRILATSREP LGIGGETALL
     IPPLPVPDPD HLPKGLPRND AVTLFVERGA AAVPGFELTE DNKVAIARIC QRLDGLPLPI
     ELAAARLRAM TPDQILRRLT DRYLLLTRGS RDAPSRQQTL RMCIDWSYDL CTPAERRMWA
     QLSVFAGSFE LEAAEQVCGC DEAEDLLDTV TFLVDKSILT REESGPAVRF RMLETLRAYG
     REKAEESGEY TELRRRHRDW CERLALEADA EWISSRQLPL IAQLGREQPN IREALEFCVS
     DSPDIGLRIA AALYPFWLSR GLFGEGRRWL GRLLDRKPPE PASDRAKALY AATVLAGVQG
     DIPVSDALAG EAQALADRTT DPMVRAHVDH TVGYAALFGG RLPDARARLE LAAEAFGGRN
     DVYEVAAIVG LGMTHDLLND TVRAIESHER VLAITEAQGE SVYRSYSLWA LAVAVWRLGE
     RARAARLLGQ ALQVDRRVND RLNASVCLQA LAWIAAEEQN MERSVVLLGA AETLARSVGS
     STVLVPGLSV YQDECERLTR GAMTEQAFAA AHRKGEAFGF DAAVAYALGE QVSAASTSAG
     PSPKPTKRER EVAALIAEGL TNKEIAARLV ISPRTAQGHV EHLLTKLGFN SRAQIAAWVV
     ESQSEGS
//
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