ID K8XTR8_RHOOP Unreviewed; 1095 AA.
AC K8XTR8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Protein kinase/ LuxR family transcriptional regulator {ECO:0000313|EMBL:EKT81512.1};
GN ORFNames=WSS_A16776 {ECO:0000313|EMBL:EKT81512.1};
OS Rhodococcus opacus M213.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1129896 {ECO:0000313|EMBL:EKT81512.1, ECO:0000313|Proteomes:UP000005951};
RN [1] {ECO:0000313|EMBL:EKT81512.1, ECO:0000313|Proteomes:UP000005951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M213 {ECO:0000313|EMBL:EKT81512.1,
RC ECO:0000313|Proteomes:UP000005951};
RX PubMed=23409266;
RA Pathak A., Green S.J., Ogram A., Chauhan A.;
RT "Draft Genome Sequence of Rhodococcus opacus Strain M213 Shows a Diverse
RT Catabolic Potential.";
RL Genome Announc. 1:E00144-12(2013).
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};
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:EKT81512.1}.
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DR EMBL; AJYC02000055; EKT81512.1; -; Genomic_DNA.
DR RefSeq; WP_005257763.1; NZ_AJYC02000055.1.
DR AlphaFoldDB; K8XTR8; -.
DR Proteomes; UP000005951; Unassembled WGS sequence.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IPR002182; NB-ARC.
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; PF00931; NB-ARC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13424; TPR_12; 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:EKT81512.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EKT81512.1}.
FT DOMAIN 26..291
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1023..1088
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1095 AA; 119401 MW; FA3458D116271517 CRC64;
MTDIDPFATQ RDASGSVTAD LAAAGFEDAH EIGRGGFGVV YRCTQAALDR TVAIKVLTAD
LDEQNRERFV REQRAAGRLT GHPNVVNVLH VGVTDHGRPY IVMPYHAQDS LDARIRRHGP
LPLDEALRLG VKMAGALETA HRLGILHRDV KPGNILLSDY GEPALSDFGI ARIAGGFETT
AGVVTGSPAF TAPEVVTGQP PSAAADVYGL GATLFAAMTG HAAFERRSGE QVVAQFLRIA
AEPGPDPRKH GVPEDVSAII ERAMTGTPED RPSATELGQQ LRASQRLHGF PVDEMALHAE
AGAVQPQENV RVPPPHQLVS HAHDFFREVT SFVGRRNEVA AVKARLSDSR IVTLTGFGGV
GKTRLACRVA SEVRRTYTDG VWFVDLAAIS TPELVVSAIT EALDIRDGMT ADGSHYLFEF
LGGRHALIVL DNCEHLIEAS GSVAVDIVRR SDRVEILATS REPLGVLGEA VFEVPPMPVP
EEAQLADGQN AKSFHSEAVD LFEQRAAAVV PGYTLDDESR LEVARLCQRL DGIPLAIELA
AVRIRSLPLD RVLSREGALF EILTRGNRGG PVRHQTLRGA IDWSFNLCSP EEQVLWARLS
VFAGGFDFDA VESVCTDPNI VSDAFDLISS LVEKSVISTV QSGSTVRYKL LESIKDYAAE
KLAEQRDADT WRRNHRDYFL HLAELSESQS LGSGQLVWNR RLRHERANLR AALEYCLSTP
GEARTGLRMA GALWFFWNAS GLLRDGRYWL TRALETDQDP SSERAKALWV IAWNAMVQGD
NPTSKQYLLE CSAVAEAIGD RTAQAFAVQF RGAAEMLGNG NLDVALENLT AGMALHAESG
EVNSLTLLGG AQLALVHCLS GNLEQSLAWA DETIASGKSL REHFSTSWAL WARGLALWTQ
RKYPQASDSL KESLELKQSL SDWLGVSTCT EILAWIAIEE ANPVRSARLL GIGRTLCGEM
GSSPLFGNDT LIRTRTRYEQ RTRQLLGDSA FEKEFRAGER LEHLASIEFA LQKRTSQPAA
AATPAAKVKL TPREKEVGNL VAEGLTNKEI AERLVISPRT AEGHVDRILT KTGHRSRAQL
AAWIAREESI ESRNP
//