ID   Q0S4C2_RHOJR            Unreviewed;      1165 AA.
AC   Q0S4C2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
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   OrderedLocusNames=RHA1_ro05837 {ECO:0000313|EMBL:ABG97614.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97614.1, 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|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|PIRNR:PIRNR000574};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000574}.
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DR   EMBL; CP000431; ABG97614.1; -; Genomic_DNA.
DR   RefSeq; WP_011597940.1; NC_008268.1.
DR   AlphaFoldDB; Q0S4C2; -.
DR   KEGG; rha:RHA1_ro05837; -.
DR   PATRIC; fig|101510.16.peg.5877; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_2_0_11; -.
DR   OrthoDB; 136365at2; -.
DR   Proteomes; UP000008710; Chromosome.
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; IPR016236; Ser/Thr_kinase_PknK_prd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000574, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000574, ECO:0000313|EMBL:ABG97614.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000574, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000574};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000574, ECO:0000313|EMBL:ABG97614.1}.
FT   DOMAIN          36..293
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          313..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1165 AA;  127698 MW;  1831132282B22A99 CRC64;
     MPRHPESSSG PTDSDPQATK RIVVTDIVAE LSSEGFDDAR EIGRGGFGVV YRCLQTALDR
     TVAIKVLSSD LDGEDRERFL REQRAMGKLS GHPHVVDILQ SGVTRSGRPY IVMPYHSRNS
     LDAWIRREGP LPWSETLRVG VKLAGALETA HRLGTLHRDV KPANILLTGY GEPQLTDFGI
     ARVTGGFETT SSMITGSPAF TAPEVLRGDA PSAASDVYSL GAALFCLLTG HAAFERRSGE
     RLVAQFLRIA TQPVPDLRGE DIPDDVCSAI ERAMSEEPTD RPASAAEFGQ ELRDIERRHG
     LDVDEMALPA AADEFPRTEH TSTPTTQSST SGHSRSYRRR SGATPPSAAA RFRPPTPMRS
     LVERTRLLDL LRMGQRRRLT LIHAPAGFGK STVAAQWRDV LIEDGAAVAW LTVDNDDNNV
     VWFLSHLVEA IRRADPTLAD ELGQALDENG AEAERYVLTS LVNQVHDSRR HVVVMIDDWH
     RVTSPDTIAA MDFILENGCH HLQMVVSSRS QAGLPLAKMR VRDELVEIDS VALRFDITES
     QRFLVDLGGL HLEDSDVEAL EETTDGWVAA LQLASLSLRD RADPGDLIRH MSGRHHAIGE
     YLAENVLSTL EPALLDFMLA TSVTERVCGD LACVLANVTR GQALLEQVES RDLFLRSLDE
     DREWFEYHHL FAEYLRRRLE RDHPSRIADL HRAAAHWFAD HHYVSDAVDH ALAAGDRDVA
     VAVVEEQGMY LVEHSRMIAL LGLVDKLPRP LVESSPRIQI AVAWANILLQ RVAPTLRSLS
     LVASALESST LNDTEQADIR VEADIVRAVI AVSSDRIAGV PDLIAECLAR PETLRAWVVS
     AGSNLASAVA IAQFDFVEAR RLQDWATGYH QRTVGPFSRM YGYSFAGIAA MEQLDIAAAE
     DNFRLAVQTA TKLAGTHSHA ARLAGALLGE LMYELGHLDE AERLLDESYE LGPEGGIVDF
     MIARFVTGAR LKASRGDLAS AARHLDEGAS AAASLGLPRL RARVENERVR LGLPASPQPP
     AGDGKATRVP DFGFAEIVAQ LDAATEIRKQ SAVEPDVACR RAEEWVRRVE RESRPRAAMQ
     ASRLLVACLV AAGRVDEAKP VLASIAATCA RIGFVRYLID GGPRMVPALT ALLEDRRAGR
     WQSDWPDVPE EFLVAALETA TPIES
//