ID PKNF_MYCBO Reviewed; 476 AA. AC Q7TZN1; A0A1R3XZ88; X2BJ00; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Serine/threonine-protein kinase PknF; DE EC=2.7.11.1; GN Name=pknF; OrderedLocusNames=BQ2027_MB1775; 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 -!- PTM: Dephosphorylated by PstP. {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; SIU00378.1; -; Genomic_DNA. DR RefSeq; NP_855427.1; NC_002945.3. DR RefSeq; WP_010950588.1; NC_002945.4. DR AlphaFoldDB; Q7TZN1; -. DR SMR; Q7TZN1; -. DR PATRIC; fig|233413.5.peg.1939; -. DR Proteomes; UP000001419; 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; 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; 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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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..476 FT /note="Serine/threonine-protein kinase PknF" FT /id="PRO_0000171212" FT DOMAIN 12..279 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 332..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..376 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 137 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 18..26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 8 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 13 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 173 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 175 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 287 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 290 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 476 AA; 50698 MW; FD16541A9139163C CRC64; MPLAEGSTFA GFTIVRQLGS GGMGEVYLAR HPRLPRQDAL KVLRADVSAD GEYRARFNRE ADAAASLWHP HIVAVHDRGE FDGQLWIDMD FVDGTDTVSL LRDRYPNGMP GPEVTEIITA VAEALDYAHE RRLLHRDVKP ANILIANPDS PDRRIMLADF GIAGWVDDPS GLTATNMTVG TVSYAAPEQL MGNELDGRAD QYALAATAFH LLTGSPPFQH ANPAVVISQH LSASPPAIGD RVPELTPLDP VFAKALAKQP KDRYQRCVDF ARALGHRLGG AGDPDDTRVS QPVAVAAPAK RSLLRTAVIV PAVLAMLLVM AVAVTVREFQ RADDERAAQP ARTRTTTSAG TTTSVAPAST TRPAPTTPTT TGAADTATAS PTAAVVAIGA LCFPLGSTGT TKTGATAYCS TLQGTNTTIW SLTEDTVASP TVTATADPTE APLPIEQESP IRVCMQQTGQ TRRECREEIR RSNGWP //