ID PKAB_STRCO Reviewed; 417 AA. AC P54740; Q9L061; Q9L1S2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Serine/threonine-protein kinase PkaB; DE EC=2.7.11.1; GN Name=pkaB; OrderedLocusNames=SCO2973; ORFNames=SCE50.01, SCE59.32c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A3(2) / NRRL B-16638; RX PubMed=7883195; DOI=10.1016/0378-1119(94)00789-u; RA Urabe H., Ogawara H.; RT "Cloning, sequencing and expression of serine/threonine kinase-encoding RT genes from Streptomyces coelicolor A3(2)."; RL Gene 153:99-104(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(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 mainly at Thr. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D86821; BAA13169.1; -; Genomic_DNA. DR EMBL; AL939114; CAD55460.1; -; Genomic_DNA. DR PIR; JC4071; JC4071. DR RefSeq; NP_733588.1; NC_003888.3. DR RefSeq; WP_011028691.1; NZ_VNID01000010.1. DR AlphaFoldDB; P54740; -. DR SMR; P54740; -. DR STRING; 100226.gene:17760585; -. DR PaxDb; 100226-SCO2973; -. DR PATRIC; fig|100226.15.peg.3031; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR InParanoid; P54740; -. DR OrthoDB; 9762169at2; -. DR PhylomeDB; P54740; -. DR BRENDA; 2.7.11.1; 5998. DR Proteomes; UP000001973; 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; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..417 FT /note="Serine/threonine-protein kinase PkaB" FT /id="PRO_0000171233" FT DOMAIN 9..270 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 279..371 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 395..417 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 130 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 36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 417 AA; 43417 MW; 3D66720FF17D3DE4 CRC64; MARKIGSRYT AHQILGRGSA GTVWLGEGPD GPVAIKLLRE DLASDQELVS RFVQERTALL GLDHPHVVSV RDLVVDGNDL ALVMDLVRGT DLRTRLDRER RLAPEAAVAV VADVADGLAA AHAAGVVHRD VKPENVLLDM QGPLGPGGSH PALLTDFGVA KLIDTPRRTR ATKIIGTPDY LAPEIVEGLP PRAAVDIYAL ATVLYELLAG FTPFGGGHPG AVLRRHVTET VVPLPGIPDE LWQLLVQCLA KAPASRLRAS ELSARLRELL PMLAGMAPLD VDEPDAEQPE DAPDASAASP AAPVSTAEPV RRRGAVPLVP GAKPADSNRD THTSMRVPAP DELAGGARGT ARAPRASGAP RPGSARNRAA TRRRRIAVGA GAVALVAAIG VGTWLATGGD EDGGGPQDTR NSAPAAP //