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
//