ID PKNJ_MYCBO Reviewed; 589 AA. AC P65733; A0A1R3Y092; Q10697; X2BK37; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Serine/threonine-protein kinase PknJ; DE EC=2.7.11.1; GN Name=pknJ; OrderedLocusNames=BQ2027_MB2115; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane CC protein {ECO:0000250}. 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; LT708304; SIU00722.1; -; Genomic_DNA. DR RefSeq; NP_855764.1; NC_002945.3. DR RefSeq; WP_003410735.1; NC_002945.4. DR AlphaFoldDB; P65733; -. DR SMR; P65733; -. DR PATRIC; fig|233413.5.peg.2325; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.40.1000.70; PknH-like extracellular domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR026954; PknH-like_Extracell. DR InterPro; IPR038232; PknH-like_Extracell_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF14032; PknH_C; 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; Cell membrane; Kinase; Membrane; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..589 FT /note="Serine/threonine-protein kinase PknJ" FT /id="PRO_0000171221" FT TOPO_DOM 1..342 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 364..589 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 14..276 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 365..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 365..392 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 20..28 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 589 AA; 61595 MW; E1E179150E2D348E CRC64; MAHELSAGSV FAGYRIERML GAGGMGTVYL ARNPDLPRSE ALKVLAAELS RDLDFRARFV READVAAGLD HPNIVAVHQR GQFEGRLWIA MQFVDGGNAE DALRAATMTT ARAVYVIGEV AKALDYAHQQ GVIHRDIKPA NFLLSRAAGG DERVLLSDFG IARALGDTGL TSTGSVLATL AYAAPEVLAG QGFDGRADLY SLGCALFRLL TGEAPFAAGA GAAVAVVAGH LHQPPPTVSD RVPGLSAAMD AVIATAMAKD PMRRFTSAGE FAHAAAAALY GGATDGWVPP SPAPHVISQG AVPGSPWWQH PVGSVTALAT PPGHGWPPGL PPLPRRPRRY RRGVAAVAAV MVVAAAAVTA VTMTSHQPRT ATPPSAAALS PTSSSTTPPQ PPIVTRSRLP GLLPPLDDVK NFVGIQNLVA HEPMLQPQTP NGSINPAECW PAVGGGVPSA YDLGTVIGFY GLTIDEPPTG TAPNQVGQLI VAFRDAATAQ RHLADLASIW RRCGGRTVTL FRSEWRRPVE LSTSVPEVVD GITTMVLTAQ GPVLRVREDH AIAAKNNVLV DVDIMTPDTS RGQQAVIGIT NYILAKIPG //