ID   PKSC_STRCO              Reviewed;         556 AA.
AC   Q9S2C0; Q9ZFS8;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Serine/threonine-protein kinase PksC;
DE            EC=2.7.11.1;
GN   Name=pksC; OrderedLocusNames=SCO3821; ORFNames=SCGD3.22;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Bakal C.J., Davies J.E.;
RT   "Cloning, nucleotide sequence and expression of a serine/threonine protein
RT   kinase gene from Streptomyces coelicolor.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF094711; AAC64406.1; -; Genomic_DNA.
DR   EMBL; AL939117; CAB46944.1; -; Genomic_DNA.
DR   PIR; T36502; T36502.
DR   PIR; T42100; T42100.
DR   RefSeq; NP_628010.1; NC_003888.3.
DR   RefSeq; WP_011029251.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9S2C0; -.
DR   SMR; Q9S2C0; -.
DR   STRING; 100226.gene:17761445; -.
DR   PaxDb; 100226-SCO3821; -.
DR   DNASU; 1099257; -.
DR   PATRIC; fig|100226.15.peg.3889; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   InParanoid; Q9S2C0; -.
DR   OrthoDB; 9762169at2; -.
DR   PhylomeDB; Q9S2C0; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005524; F:ATP 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; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 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; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..556
FT                   /note="Serine/threonine-protein kinase PksC"
FT                   /id="PRO_0000171236"
FT   DOMAIN          20..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          482..550
FT                   /note="PASTA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          300..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..350
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         26..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        80
FT                   /note="I -> M (in Ref. 1; AAC64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="I -> L (in Ref. 1; AAC64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="G -> C (in Ref. 1; AAC64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="L -> V (in Ref. 1; AAC64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="P -> L (in Ref. 1; AAC64406)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   556 AA;  58262 MW;  D4A22A2F39F4ADC1 CRC64;
     MSQDGGQGRY AGRALAGGRY QLRDLLGEGG MASVHLAYDS VLDRQVAIKT LHTELGREQA
     FRERFRREAQ AVAKLTHTNI VSVFDTGEDD LDGMTTPYIV MEYVEGRPLG SVLDEDVRQQ
     GAMPADKALK ITADVLAALE ISHEMGLVHR DIKPGNVMMT KRGVVKVMDF GIARAMQSGV
     TSMTQTGMVV GTPQYLSPEQ ALGRGVDARS DLYSVGIMLF QLVTGRLPFD ADSPLAIAYA
     HVQEQPVAPS AVNRALPPAV DALVARALKK NPNERFPSAE AMRDECLRVA ASFQAAPPSI
     VPGAQTSSGA GVGSAVFPPV GQGTPAPTGP VQTPYQPTPS PGPNPYGTPA PAAHSPAYGY
     PQQAGYQTPA PAPYAQQQAA ATPPPYNLTP SAQGSGSGSP GGKSNKPVII GSIVVAVVAV
     GGLIGALLMN GGGDEDPEAG GGGSSTASVS ASPSKAAGYR GPDKEKTIEK DKCTEPQESY
     NDPDKIQVPD FTFKYIGSVK ECFNAAGWQM KVVEVDENTY GEGSVRDQFP TAGTDVDPEN
     MPEIQLKVST GNPPSE
//