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 27-MAR-2024, entry version 122.
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; Bacillota; 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 KEGG; cpe:CPE1738; -.
DR HOGENOM; CLU_000288_135_2_9; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
