ID A1R0U7_PAEAT Unreviewed; 637 AA. AC A1R0U7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=AAur_0028 {ECO:0000313|EMBL:ABM08627.1}; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08627.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM08627.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM08627.1, RC ECO:0000313|Proteomes:UP000000637}; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H., RA Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter RT aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). 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; CP000474; ABM08627.1; -; Genomic_DNA. DR RefSeq; WP_011772807.1; NC_008711.1. DR AlphaFoldDB; A1R0U7; -. DR STRING; 290340.AAur_0028; -. DR KEGG; aau:AAur_0028; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000000637; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABM08627.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABM08627.1}; KW Transferase {ECO:0000313|EMBL:ABM08627.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 375..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 27..295 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 405..471 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 472..541 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 542..606 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 342..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 606..637 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 609..637 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 637 AA; 67319 MW; B0AB2AB0B99F71F8 CRC64; MSTSRPGPAH REESTPVSSQ RILNSRYELG ELIGRGGMAD VYRGTDTLLG RTIAVKVLRA DLARDPQFQA RFKREAQAVA ALNHPSIVAI FDTGEYSVPG GPGEDVRVPY IVMEYVAGRT LRDMIKANEL GVEDSVGFTL GVLGALEYSH RAGIVHRDIK PANVMVCADT GDVKVMDFGI ARAMADSAAT MTQTQAVVGT AQYLSPEQAR GETVDARSDL YSAGCLLFEL LTSRPPFIGD SPVSVAYQHV RETPDLASAH NPEVSEALDS VLVKALQKSR TDRFQDAAAF RRALRAASNG IPVPAVAASE APTDPNDLVD PEDPATELLS TTAVGFLDAD QFKDEPTDQP QEEPLPLGLP PEREVPERQK SRRRAWVATL VIFTVLVLAG GGFWLYSLMN MQPPPPAKIA VPVVTNMSES QAIQALYSAK LKPTSVREPS DTVAKDMTIG TSPIAGAMLE QDAEVVLKIS SGPSSVTIPA DIVGRTEPDA REALRRLGIT GEVVTALTHS PTVPAGVVLG TAPAPGGAIA VESKVELQVS TGKVLMPQLI ALPAAEAEAA LKANGLNIAI VEQENSQVAA GTVTAQSDAF NTEVAQGKVV TVTVAKAPAP VPTPTPTPTP TETEKPTPKP TPTPTKK //