ID Q9S2N3_STRCO Unreviewed; 667 AA. AC Q9S2N3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 128. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=pkaF {ECO:0000313|EMBL:CAB51958.1}; GN OrderedLocusNames=SCO2110 {ECO:0000313|EMBL:CAB51958.1}; GN ORFNames=SC6E10.04 {ECO:0000313|EMBL:CAB51958.1}; 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 {ECO:0000313|EMBL:CAB51958.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB51958.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; 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., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J., 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 Evidence={ECO:0000256|ARBA:ARBA00001433}; 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; Evidence={ECO:0000256|ARBA:ARBA00000775}; 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; AL939111; CAB51958.1; -; Genomic_DNA. DR PIR; T35491; T35491. DR RefSeq; NP_626367.1; NC_003888.3. DR AlphaFoldDB; Q9S2N3; -. DR STRING; 100226.gene:17759708; -. DR PaxDb; 100226-SCO2110; -. DR DNASU; 1097544; -. DR PATRIC; fig|100226.15.peg.2144; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_11; -. DR InParanoid; Q9S2N3; -. DR OrthoDB; 9762169at2; -. DR PhylomeDB; Q9S2N3; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd06577; PASTA_pknB; 4. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 4. 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; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF03793; PASTA; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 4. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:CAB51958.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAB51958.1}; KW Transferase {ECO:0000313|EMBL:CAB51958.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379..398 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 28..290 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 400..467 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 468..534 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 535..602 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 603..667 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 304..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 570..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 667 AA; 70788 MW; 1E5B598E43A5B7F0 CRC64; MSVAARTLTC VDTTLQDPLV GQVLDGRYRV EARIAVGGMA TVYRAVDTRL DRVLALKVMH PTLATDATFV ERFIREAKSV ARLDHPNVVQ VFDQGAEGAY VYLAMEYIAG CTLRDVLRER GALRPRAALD ILEPVLAALG AAHRAGFVHR DMKPENVLIG DDGRVKVADF GLVRAVDTVT STTGAVLGTV SYLAPEQIEH GTADPRVDVY ACGVMLYEML TGAKPHDGDS PAAVLYKHLH EDVPPPSAAV PELAYELDEL VAAATARNPE IRPHDAVALL ARAREARESL STAQLDAVPP QALAAEHDNA EDRTSVIPRA LTMPRPLPVN EDDGSAGPDG RFASDGGFGA DGVNRTSRLA APPPAPSPSR RLRLRRGPLT IVVAVLLVLG IGTGVWYINS GQFTKVPPLL SKTEAQARDR LDDAGLDVGK VRHAYSDTVE RGKVISTDPG VGDRIRKNDS VSLTVSDGPD TVKLPDVTGY KLDKARTLLE DEGLEPGMVT RAFSDEVARG FVISTKPGSG TTVRAGSAVA LVVSKGSPVD VPDVTGDDLD EARAELEGAG LKVKTADERV NSEYDSGRVA RQTPEPGGRA AEGDTVTLTV SKGPRMIEVP DVVGDSVDDA KQKLEDAGFE VDEDRGLLGL FGDTVKKQSV DGGDTAPEGS TVTITIR //