ID   AFSK_STRCO              Reviewed;         799 AA.
AC   P54741; Q9F365; Q9L002;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Serine/threonine-protein kinase AfsK;
DE            EC=2.7.11.1;
GN   Name=afsK; OrderedLocusNames=SCO4423; ORFNames=SC6F11.21, SCD6.01;
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;
RX   PubMed=8063104; DOI=10.1016/0378-1119(94)90832-x;
RA   Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.;
RT   "Phosphorylation of the AfsR protein involved in secondary metabolism in
RT   Streptomyces species by a eukaryotic-type protein kinase.";
RL   Gene 146:47-56(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8635757; DOI=10.1016/0378-1119(95)00771-7;
RA   Ueda K., Umeyama T., Beppu T., Horinouchi S.;
RT   "The aerial mycelium-defective phenotype of Streptomyces griseus resulting
RT   from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor
RT   A3(2).";
RL   Gene 169:91-95(1996).
RN   [3]
RP   SEQUENCE REVISION TO 239-240.
RA   Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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).
RN   [5]
RP   INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-44.
RX   PubMed=11544211; DOI=10.1128/jb.183.19.5506-5512.2001;
RA   Umeyama T., Horinouchi S.;
RT   "Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is
RT   inhibited by KbpA, an AfsK-binding protein.";
RL   J. Bacteriol. 183:5506-5512(2001).
RN   [6]
RP   PHOSPHORYLATION AT SER-71 AND THR-168, AND MUTAGENESIS OF SER-71; SER-128;
RP   THR-168 AND THR-170.
RX   PubMed=16629414; DOI=10.1038/ja.2006.18;
RA   Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M.,
RA   Ohnishi Y., Horinouchi S.;
RT   "Self-activation of serine/threonine kinase AfsK on autophosphorylation at
RT   threonine-168.";
RL   J. Antibiot. 59:117-123(2006).
CC   -!- FUNCTION: Involved in the regulation of secondary metabolism by
CC       phosphorylating, on both Ser and Thr, the AfsR global regulatory
CC       protein involved in the control of secondary metabolism.
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   -!- SUBUNIT: Interacts (via the N-terminal kinase domain) with KbpA; the
CC       interaction prevents autophosphorylation of AfsK.
CC       {ECO:0000269|PubMed:11544211}.
CC   -!- PTM: Autophosphorylated mainly on threonine residues. Some
CC       phosphorylation on serine residues. Autophosphorylation on Thr-168 is
CC       the major site enhancing kinase activity towards AfsR, and is regulated
CC       though interaction with KbpA. {ECO:0000269|PubMed:16629414}.
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; D45382; BAA08229.2; -; Genomic_DNA.
DR   EMBL; AL939120; CAD55483.1; -; Genomic_DNA.
DR   RefSeq; NP_733637.1; NC_003888.3.
DR   RefSeq; WP_011029643.1; NZ_VNID01000017.1.
DR   AlphaFoldDB; P54741; -.
DR   SMR; P54741; -.
DR   STRING; 100226.gene:17762068; -.
DR   iPTMnet; P54741; -.
DR   PaxDb; 100226-SCO4423; -.
DR   PATRIC; fig|100226.15.peg.4492; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1520; Bacteria.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   InParanoid; P54741; -.
DR   OrthoDB; 9762169at2; -.
DR   BRENDA; 2.7.11.1; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IEA:UniProtKB-KW.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.40.10.480; -; 3.
DR   Gene3D; 2.40.128.630; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR22983; PROTEIN KINASE RELATED; 1.
DR   PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..799
FT                   /note="Serine/threonine-protein kinase AfsK"
FT                   /id="PRO_0000171234"
FT   DOMAIN          16..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          295..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..343
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..423
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         22..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         71
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MOD_RES         168
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         44
FT                   /note="K->A: No autophosphorylation. Binds KbpA."
FT                   /evidence="ECO:0000269|PubMed:11544211"
FT   MUTAGEN         71
FT                   /note="S->A: No autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         128
FT                   /note="S->A: No change in autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         168
FT                   /note="T->A: Almost completely abolishes
FT                   autophosphorylation. No enhancement of kinase activity on
FT                   AfsR. Very little constitutive kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         168
FT                   /note="T->D: Almost completely abolishes
FT                   autophosphorylation. No enhancement of kinase activity on
FT                   AfsR. Constitutive kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         168
FT                   /note="T->E: Almost completely abolishes
FT                   autophosphorylation. No enhancement of kinase activity on
FT                   AfsR. Some constitutive kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16629414"
FT   MUTAGEN         170
FT                   /note="T->D: No change in autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:16629414"
SQ   SEQUENCE   799 AA;  83788 MW;  4BE9BED4169F6F5B CRC64;
     MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF
     TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PAQAVRWLAA
     GVAEALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM
     SPEQAKDSRS VTGASDVFSL GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL
     RPLIESCMQM EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP
     AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP APVGAPDGGP
     VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP RPGVNGADPA VPAPAPAPPE
     ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV TSFEVHALDV ATGRRRFKTR DVAWSMAVAD
     GRIHASDGPT LFALDAREGA DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK
     LWEVTGAQTD FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV
     RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV TGGGVYLADY
     LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS GKGLYTLDAV TGTPKWRFQA
     GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD DGRLRWKLAT GGEITGSPVV RDGIVYACSK
     DRCVYALDAE KGTGTARTT
//