ID   PK1_STRTO               Reviewed;         641 AA.
AC   Q9KIG4;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Serine/threonine-protein kinase PK-1;
DE            Short=stoPK-1;
DE            EC=2.7.11.1;
GN   Name=spk1;
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=55952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 15009;
RA   Neu J.M., Wright G.D.;
RT   "Characterization of stoPK-1, a novel protein Thr kinase from the
RT   glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION.
RX   PubMed=11972780; DOI=10.1046/j.1365-2958.2002.02879.x;
RA   Neu J.M., MacMillan S.V., Nodwell J.R., Wright G.D.;
RT   "StoPK-1, a serine/threonine protein kinase from the glycopeptide
RT   antibiotic producer Streptomyces toyocaensis NRRL 15009, affects oxidative
RT   stress response.";
RL   Mol. Microbiol. 44:417-430(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   -!- PTM: Autophosphorylated on threonine residue(s).
CC       {ECO:0000269|PubMed:11972780}.
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; AF233851; AAF79944.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KIG4; -.
DR   SMR; Q9KIG4; -.
DR   STRING; 55952.BU52_09510; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
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   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51178; PASTA; 4.
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; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..641
FT                   /note="Serine/threonine-protein kinase PK-1"
FT                   /id="PRO_0000171238"
FT   DOMAIN          18..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          375..441
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          442..508
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          509..576
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          577..641
FT                   /note="PASTA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          317..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         24..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   641 AA;  67973 MW;  806B121FEDE109FC CRC64;
     MDTTLQDPLV GQVLDGRYRV DARIAVGGMA TVYRAVDTRL DRVLALKVMH PSLAADASFV
     ERFIREAKSV ARLAHPNVVQ VFDQGTDGAY VYLAMEYIAG CTLRDVLRER GALQPRAALD
     ILEPVLAALG AAHRAGFVHR DMKPENVLIG DDGRVKVADF GLVRAVDSVT NTTGTVLGTV
     SYLAPEQIEH GTADPRVDVY ACGILLYEML TGEKPHDGDS PAIVLYKHLH DDVPPPSAAV
     PGMAYELDEL VASATARGPE VRPHDAVALL ARARDARARL GDEQLDAVPP QALASEHDNA
     DDRTSVIPRA LTVRRPLPVN EEDEGADAAH RTSRFRSPPP LPPRGRTALR RGPMAIVIGV
     LLVLGLGAGV WYINSGQFTK VPPLLAKTEK EARDRLADAG LDAGQVSEAY SDTVERGSVA
     TDPEAGARIR TNDSVSLTLS KGPRTVRVPD LDGYPQDKAR SLLEDEGLKP GMSTREFSDS
     VPAGSVISTE PGKGTEVRAG SAVALTVSKG APVDVPDVAG DDLEDARAEL EEAGLEVKVA
     TERVTSEYDA GRVARQDPGP GGRVAEGDTV TLTLSKGPEM AEVPDVVGDS VGEAREKLEG
     AGFRVDEDRG LLGLFGDTVK GQSVDGGDSA PKGSTITIEI R