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PKN2_CLOPE
ID   PKN2_CLOPE              Reviewed;         685 AA.
AC   Q8XJL8;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable serine/threonine-protein kinase CPE1738;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=CPE1738;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; BA000016; BAB81444.1; -; Genomic_DNA.
DR   RefSeq; WP_004458146.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJL8; -.
DR   SMR; Q8XJL8; -.
DR   STRING; 195102.gene:10491002; -.
DR   EnsemblBacteria; BAB81444; BAB81444; BAB81444.
DR   KEGG; cpe:CPE1738; -.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   OMA; DPDYRYQ; -.
DR   Proteomes; UP000000818; 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; 3.
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; 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..685
FT                   /note="Probable serine/threonine-protein kinase CPE1738"
FT                   /id="PRO_0000171195"
FT   DOMAIN          10..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          376..440
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          441..508
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          513..581
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          589..648
FT                   /note="PASTA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          277..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   685 AA;  74576 MW;  75A396084485EB24 CRC64;
     MIGKILGNRY ELLQCVGEGG MSFVYKARCR KLNRFVAVKI LKDEFKNNEE IVRRFKKEAT
     AIANLSNPNV VNVLDVGTQD DINYIVMEYV EGKTLKDIIK EKGALPYEVA ISIGIKVAKA
     LECAHKSGII HRDVKPQNIL VTEEGVVKVT DFGIAKSMDS STIAHTNSVM GSAHYFSPEQ
     AKGTYTDYRT DLYSLGIVLY EMVTGVVPFN GDSPVTVAVK HIQEKAIPPK NINQNIPNSL
     NDLIMKAMEK DPVNRYQTAK EIIGDLEKIK KDPNVTISSK SAEDEDQFTR VMSPVVVPNT
     ETNNSEPDED DEDDDEYYED DEDEDEEENN IQTKPQKAIN KNKKKSPILI IIATILVVAL
     GITLGFLGMK KFMEGGKDVK IPNVVGEKVE DAKSKLEGLG LKVLEVTEES DQEKGIVLKV
     DPNVDSTVKT GSEVKLTVSG GEGQIKVPNF AEMNLDSVKR TLKSLGLELG SVDEEYSDSV
     PRGEVISQSP NANESVDKGS KVNVTISKGK EIKSETINIP DVSGKSVEEA KSILANAGVG
     VNPVKGEAAK SEGEAGKVYS QSQSGSLTIK QGEKVTITIN YYGDYVKPEK PKHNAGELVG
     MTGAQAKAWA SKNKINVSGI TSDTAKVKSV SNSGEVEEGG SVSVTMEEEK KPEQPTQPNQ
     PTQPTQPNQQ AQPEQPKQPE QSGNN
 
 
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