ID Q4JYC0_CORJK Unreviewed; 540 AA. AC Q4JYC0; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 116. DE SubName: Full=Serine/threonine protein kinase PknA {ECO:0000313|EMBL:CAI36187.1}; DE EC=2.7.1.37 {ECO:0000313|EMBL:CAI36187.1}; GN Name=pknA {ECO:0000313|EMBL:CAI36187.1}; GN OrderedLocusNames=jk0038 {ECO:0000313|EMBL:CAI36187.1}; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36187.1, ECO:0000313|Proteomes:UP000000545}; RN [1] {ECO:0000313|EMBL:CAI36187.1, ECO:0000313|Proteomes:UP000000545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K411 {ECO:0000313|EMBL:CAI36187.1, RC ECO:0000313|Proteomes:UP000000545}; RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., RA Rupp O., Schneiker S., Viehoever P., Puehler A.; RT "Complete genome sequence and analysis of the multiresistant nosocomial RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the RT human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}. 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; CR931997; CAI36187.1; -; Genomic_DNA. DR RefSeq; WP_011272803.1; NC_007164.1. DR AlphaFoldDB; Q4JYC0; -. DR STRING; 306537.jk0038; -. DR GeneID; 3432408; -. DR KEGG; cjk:jk0038; -. DR PATRIC; fig|306537.10.peg.49; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000000545; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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: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; IPR017441; Protein_kinase_ATP_BS. 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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAI36187.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000545}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAI36187.1}; KW Transferase {ECO:0000313|EMBL:CAI36187.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 383..403 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 23..283 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 288..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 444..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 487..540 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 540 AA; 57019 MW; A4EBDC71318D9165 CRC64; MSDSRQPDRT EIERTQRLLG ERFELQWIIG RGGMSTVWLA HDVEQQRDVA VKILKPEYTE NEEFRARFRN EASAAQDLDS PNVVRTYDSG EVEDPDNGTV FCYIIMEYIR GESLADVLSR ESSLPQNLAL DVLTQTAAGL KAIHEAGLVH RDIKPGNLLI TSDGFVKITD FGIAKAAAAV PLTRTGMVVG TAQYVSPEQA QGDQVGPASD VYSLGVVGFE MLAGYRPFSG ESTVSVAIKH ISETPPELPE EIDPNLRELI RVCLRKSPRT RYADGAELAT ATVMVAEGKQ PPSPHNVPNV SAEPHPLTEQ LGNVASGPGT RVPSVPGPQY GPGSGARPGQ GPGYPDSSVP VVGAGAPPTD AGYPATARGA GGAQGASPKK NRWIIAVLAL VSILALALAT FLLTSGGDKE APNPSTMTVT NEVTTSPTEE GEPANPSGNV PAPVNPSPTD TTNGPSTTSK TETSREETET SEEREPSFPT LPTIPNGGGR GNGNGNGENG TARQTEPNQP HTNDNATSED SDMPAELRSP STNPESQPVL //