ID   PKN1_COREF              Reviewed;         660 AA.
AC   Q8FUI5;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable serine/threonine-protein kinase CE0033;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=CE0033;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC16843.1; -; Genomic_DNA.
DR   RefSeq; WP_006768658.1; NZ_GG700684.1.
DR   AlphaFoldDB; Q8FUI5; -.
DR   SMR; Q8FUI5; -.
DR   STRING; 196164.23491868; -.
DR   EnsemblBacteria; BAC16843; BAC16843; BAC16843.
DR   KEGG; cef:CE0033; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OMA; DPDYRYQ; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000001409; 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   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   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51178; PASTA; 4.
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; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..660
FT                   /note="Probable serine/threonine-protein kinase CE0033"
FT                   /id="PRO_0000171196"
FT   DOMAIN          9..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          377..443
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          444..512
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          513..577
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          288..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   660 AA;  69647 MW;  D33D797EB02D44B1 CRC64;
     MTFVIADRYE LGASIGSGGM SEVFAATDLL IGREVAVKML RTDLAKDVNF RERFRREAQN
     AGKLSHPSIV AVFDTGEVDR DGISVPYIVM ERVHGRDLRD IVREDGPYSP SQAATIMIPV
     CHALQSSHEA GIIHRDVKPA NIMINNTGGV KVMDFGIARA LDDSTSAMTQ TAAVIGTAQY
     LSPEQARGKP ADARSDVYAA GCVLYELVTG RPPFEGESPF AVAYQHVQEE PTPPSEYISD
     LSPTAALNVD AVVLTAMAKH PADRYQTAAE MAADLELLSR NAVSRAARAH VEKPDEPETV
     VVPQRLSTPP PPPTPAMPAA TVAAPAAAPT AVGSRPAAAR QPKRGSRALT VLAIVLTLGV
     IGVGGAFTYD FLSNSSSAST QQIPNIVGLP ENEAVLELER LGFTVVLTTE PSPDVAEGLV
     IRTSPNVGSE IREGATVTLT ISSGREVVTI PDVTGLTLAE ATREIEGAGL VLDQSIREEN
     SDDYPAGTVI QQNPRAGGET SVGASITLTV STGPSLVRVP VITGMQWSQA ESNITSLGLV
     PDIYYVDSLL PEGQVISASG QGTELPRGST VTVEISNGML IEAPDLARLD VDNALKALRD
     AGWTAPDTSL IEGAPIPTGA LVDQGRIGFQ DPSPGQPLRK DAVVNIRLYR FDLTALVPEP