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 25-NOV-2008, entry version 70. 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. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1902; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A3(2); RX MEDLINE=94341568; 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 RT in 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); RX MEDLINE=96186909; 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 RT resulting from A-factor deficiency is suppressed by a Ser/Thr kinase RT of S. coelicolor 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., RA 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 MEDLINE=21996410; 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., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). RN [5] RP INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-44. RX PubMed=11544211; 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 AUTPOPHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, AND RP MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170. RX PubMed=16629414; 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 RT autophosphorylation at 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: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts (via the N-terminal kinase domain) with kbpA; CC the interaction prevents autophosphorylation of afsK. CC -!- PTM: Autophosphorylated mainly on threonine residues. Some CC phosphorylation on serine residues. Autophosphorylation on Thr-168 CC is the major site enhancing kinase activity towards afsR, and is CC regulated though interaction with kbpA. CC -!- MASS SPECTROMETRY: Mass=1638.8; Method=Electrospray; Range=68-93; CC Source=PubMed:16629414; CC -!- MASS SPECTROMETRY: Mass=1718.8; Method=Electrospray; Range=68-93; CC Note=Monophosphorylated; Source=PubMed:16629414; CC -!- MASS SPECTROMETRY: Mass=2236.5; Method=Electrospray; Range=117- CC 137; Source=PubMed:16629414; CC -!- MASS SPECTROMETRY: Mass=2109.4; Method=Electrospray; Range=167- CC 186; Source=PubMed:16629414; CC -!- MASS SPECTROMETRY: Mass=2189.4; Method=Electrospray; Range=167- CC 186; Note=Monophosphorylated; Source=PubMed:16629414; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D45382; BAA08229.2; -; Genomic_DNA. DR EMBL; AL939120; CAD55483.1; -; Genomic_DNA. DR RefSeq; NP_733637.1; -. DR HSSP; P71584; 1O6Y. DR GeneID; 1099863; -. DR GenomeReviews; AL645882_GR; SCO4423. DR KEGG; sco:SCO4423; -. DR NMPDR; fig|100226.1.peg.4378; -. DR HOGENOM; P54741; -. DR LinkHub; P54741; -. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR011047; Quino_AlcDHase-like. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 2. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00564; PQQ; 9. 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; Complete proteome; Kinase; Nucleotide-binding; KW Phosphoprotein; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 799 Serine/threonine-protein kinase afsK. FT /FTId=PRO_0000171234. FT DOMAIN 16 271 Protein kinase. FT NP_BIND 22 30 ATP (By similarity). FT COMPBIAS 317 428 Pro-rich. FT ACT_SITE 138 138 Proton acceptor (By similarity). FT BINDING 44 44 ATP (By similarity). FT MOD_RES 71 71 Phosphoserine; by autocatalysis. FT MOD_RES 168 168 Phosphothreonine; by autocatalysis. FT MUTAGEN 44 44 K->A: No autophosphosphorylation. Binds FT kbpA. FT MUTAGEN 71 71 S->A: No autophosphorylation. FT MUTAGEN 128 128 S->A: No change in autophosphorylation. FT MUTAGEN 168 168 T->A: Almost completely abolishes FT autophosphorylation. No enhancement of FT kinase activity on afsR. Very little FT constitutive kinase activity. FT MUTAGEN 168 168 T->D: Almost completely abolishes FT autophosphorylation. No enhancement of FT kinase activity on afsR. Constitutive FT kinase activity. FT MUTAGEN 168 168 T->E: Almost completely abolishes FT autophosphorylation. No enhancement of FT kinase activity on afsR. Some FT constitutive kinase activity. FT MUTAGEN 170 170 T->D: No change in autophosphorylation. 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 //