PKN2_CLOAB
ID PKN2_CLOAB Reviewed; 657 AA.
AC Q97IC2;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable serine/threonine-protein kinase CA_C1728;
DE EC=2.7.11.1;
GN OrderedLocusNames=CA_C1728;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79694.1; -; Genomic_DNA.
DR PIR; C97113; C97113.
DR RefSeq; NP_348354.1; NC_003030.1.
DR RefSeq; WP_010965035.1; NC_003030.1.
DR AlphaFoldDB; Q97IC2; -.
DR SMR; Q97IC2; -.
DR STRING; 272562.CA_C1728; -.
DR EnsemblBacteria; AAK79694; AAK79694; CA_C1728.
DR GeneID; 44998223; -.
DR KEGG; cac:CA_C1728; -.
DR PATRIC; fig|272562.8.peg.1930; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OMA; DPDYRYQ; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000000814; 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; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51178; PASTA; 3.
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..657
FT /note="Probable serine/threonine-protein kinase CA_C1728"
FT /id="PRO_0000171194"
FT DOMAIN 10..274
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 443..509
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 512..577
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 286..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Basic and acidic 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 657 AA; 71115 MW; 0901452EF42E2CA6 CRC64;
MIGTVLSNRY KIEEEIGVGG TAVVYKAMDT LLNRHVAVKV LKHEFTEDEE FVFKFKREAS
AAARIANANI VNIYDVGADG NVNYIVMEYV AGKTLKKLIK ENGKIEFNKI IDYATQIAKA
LNFAHKNGIV HRDIKPHNIM VTDDDIIKVT DFGIAKASNE STITTTNKVV GSAHYLSPEQ
AQGIPVDCRT DIYSFGIVLY EMATGKVPYD ADTPVSIALK HIQDAAVPPN ELNKDIPIAL
NKMILRCIEK KPENRYQNAN EILDELSNVK NNYVNDDEEF TRVMDPAQIQ NESNPNNKLD
NDDTYYNGEP YNKEQPQEEP QEENEEPKNK IKGNNMLSGK AKKALVASII VVLILAGSAL
AFSMGSGIFK PNSNSVSKVK VPKIIGLSES DAKGKVEDAK LKFQVVDRVK SSKPKGTVVT
CYPNEDTEVD SGTVVRVDIS SGDTDQTLPS LVGLPESAAR AQIKQYGCNV GSVTQEYSDD
VAQGNVISQS PSEGSQIKKG MTIDLVISRG PEVKKATVPS VYGKTSDSAS SILQNAGFGV
NVQNKDVTNA DQNGIVIEEY PNGYVNKGTT VTIVIGRFNS TAVQPPNNNN GNGNQNQNQN
KTPDTNHDDS KAPTGGNNDN QNQNNTTNPN GTQPAGGNVT GTGNGNVTNT PNGTGQK
