ID   Q0S014_RHOJR            Unreviewed;      1180 AA.
AC   Q0S014;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Serine/threonine-protein kinase PknK {ECO:0000256|PIRNR:PIRNR000574};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000574};
DE   AltName: Full=Protein kinase K {ECO:0000256|PIRNR:PIRNR000574};
GN   Name=pknK1 {ECO:0000313|EMBL:ABG99122.1};
GN   OrderedLocusNames=RHA1_ro08075 {ECO:0000313|EMBL:ABG99122.1};
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL1 {ECO:0000313|EMBL:ABG99122.1,
OG   ECO:0000313|Proteomes:UP000008710}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG99122.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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         ECO:0000256|PIRNR:PIRNR000574};
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         ECO:0000256|PIRNR:PIRNR000574};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00038035}.
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DR   EMBL; CP000432; ABG99122.1; -; Genomic_DNA.
DR   RefSeq; WP_011599017.1; NC_008269.1.
DR   AlphaFoldDB; Q0S014; -.
DR   KEGG; rha:RHA1_ro08075; -.
DR   PATRIC; fig|101510.16.peg.7419; -.
DR   HOGENOM; CLU_006325_2_0_11; -.
DR   Proteomes; UP000008710; Plasmid pRHL1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   InterPro; IPR041664; AAA_16.
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; IPR016236; Ser/Thr_kinase_PknK_prd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR48013:SF35; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 4; 1.
DR   PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   PIRSF; PIRSF000574; Ser/Thr_PK_PknK_prd; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000574};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000574};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000574}; Plasmid {ECO:0000313|EMBL:ABG99122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000574};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000574}.
FT   DOMAIN          26..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          298..352
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   1180 AA;  127881 MW;  B723F150D7E165E5 CRC64;
     MTNEDGPGPG RGLVPVLKAE LEADGFAEVS EIGHGGFGVV FRCREPSLDR TVAVKVLNST
     FDEDGYARFL REQRAMGQLS GHPNIVNVLR IGATASGRQF LVMQYHARGS LDAVLRSRGP
     LEWSAAVRIG VKLAGALETA HRAGILHRDI KPGNVLLTSY GEPQLSDFGI ARIAGGFETD
     TGTITGSPAF TAPEVLSGDP PTLASDVYGL GATLFCLLTG HAAFERRSGE QIVAQFLRIA
     AESAPRLPAA GIPADVRAAV ESAMARDPGR RPGTAAEFGH QLRTIEASHG LTADEMALPQ
     DSHPAAPDPS PRHDTGTVDY APTELGQRAE VDEPPRQPPS ASTKYRPPTP SRALVERGRL
     AERLHDAARR RLILIHAPAG FGKSTLAAQW RRTLADDGVA VAWLSIDADD NNVVWFLSHL
     IESIRVVRPD LAAELGQILD DHGDESDRFV LTALINEIHT SRDPLTVVID DWHLVTDPAT
     IAAMSFLLDN GCHHLQVMVT SRSQSGLPLG RMRVRDELVE IDSTALRFDE EESRQFLVDV
     GGLALDRDAI SALRDSTEGW VAALQLATLS LRGRDDPAEF IAHLSGRHRG IAGYLAENVL
     SALEPEILDF MLATSVTERL CADLAETLAG VAGGQGLLEQ IEERDLFLRA LDDDREWFRY
     HHLFADFLRR RLQRDQPSRI ADLHRTASRW FAAHELLSEA VDQSLAAADP DQAAELVDSR
     GFALIERSQM ATVLGLIGKL LPAQIERRPH LQIAAAWAHI LLHHRPTIVD SALDSVRVGL
     AALPESGNAT AALRAEASLV QAAADLFRDR IDDLTELISD CLAREKTLRP FALAGSANVA
     SYEAIHRFDF EAAKRWQEWA APFHARTSGP FSVIYGYCLS GLAESELLNV QEAEDYYRKA
     YDLARRSGGH RSYTTRLAGT MLGESLYEQG LLDDAERLLD ECSELGSEGG VVDFMLVTFG
     TGSRIKALRG DLAAAAHRLD EGTQIATALS LPRLAARIEN ERTRWRIAPG QYPQAMTMAS
     ALPDTAAPTS HPVNGVNGVI EVTAELNEDS AIRRLLASGD PGDAALAHRR AEQLLARATA
     LHRPRATLRA SLLHVVTTRR VQGEHDALAA LVPLVAQCSR LGLIRPLCDE GPALTRLVAT
     LVELHESQDW DAGWPAVSAP FLRAVLASSD ATSPPPHAPD
//