AFSK_STRCO
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 03-AUG-2022, entry version 149.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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.SCO4423; -.
DR iPTMnet; P54741; -.
DR GeneID; 1099863; -.
DR KEGG; sco: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 OMA; PKWRFQA; -.
DR BRENDA; 2.7.11.1; 5998.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025666; PQQ-like_dom.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 2.
DR SMART; SM00564; PQQ; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF56112; SSF56112; 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
