ID PKAA_STRCO Reviewed; 543 AA. AC P54739; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Serine/threonine-protein kinase PkaA; DE EC=2.7.11.1; GN Name=pkaA; OrderedLocusNames=SCO2974; ORFNames=SCE50.02c; 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 and slightly at Ser. 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; BAA13168.1; -; Genomic_DNA. DR EMBL; AL939114; CAB87324.1; -; Genomic_DNA. DR PIR; JC4070; JC4070. DR RefSeq; NP_627197.1; NC_003888.3. DR RefSeq; WP_003975838.1; NZ_VNID01000010.1. DR AlphaFoldDB; P54739; -. DR SMR; P54739; -. DR STRING; 100226.gene:17760586; -. DR PaxDb; 100226-SCO2974; -. DR PATRIC; fig|100226.15.peg.3032; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR InParanoid; P54739; -. DR OrthoDB; 9762169at2; -. DR PhylomeDB; P54739; -. 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; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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..543 FT /note="Serine/threonine-protein kinase PkaA" FT /id="PRO_0000171232" FT DOMAIN 8..276 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 303..480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..368 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..396 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..431 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..447 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..463 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 142 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 14..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 543 AA; 58182 MW; 0E1965520FA0C200 CRC64; MRPVGSKYLL EEPLGRGATG TVWRARQRET AGAEAAVAGQ PGETVAIKVL KEELASDADI VMRFLRERSV LLRLTHPNIV RVRDLVVEGE LLALVMDLID GPDLHRYLRE NGPLTPVAAA LLTAQIADAL AASHADGVVH RDLKPANVLL KQTGGEMHPM LTDFGIARLA DSPGLTRTHE FVGTPAYVAP ESAEGRPQTS AVDVYGAGIL LYELVTGRPP FGGGSALEVL HQHLSAEPRR PSTVPDPLWT VIERCLRKNP DDRPSAENLA RGLRVVAEGI GVHANSAQIG AAENVGALLA PDPAPAQVPG APDAAYDPNG ATSVLPHTSG PAGAADPTAV LPSTGAPDPT AVMPPVPPGQ PGAPGQGGPE DPHPWQNQLR AARDRNEQTQ VQYLDPNQDP LRRRPQRQVS RPPQQPRQAP QGPPPQQPGY GYPQQQQPQR YATPQPQQPQ RYAPPPAPEP QQPRREPRPP RQRSANPMRI PGLGCLKGCL VTVVVLFVAG WLVWELSPLQ EWIGTGKGYW DQLTDWFTTV TDWIGDLGGS GGG //