ID PKNB_MYCS2 Reviewed; 625 AA. AC A0QNG1; DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Serine/threonine-protein kinase PknB; DE EC=2.7.11.1; GN Name=pknB; OrderedLocusNames=MSMEG_0028, MSMEI_0031; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20; RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.; RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic RT mutations or sequencing errors?"; RL Genome Biol. 8:R20.1-R20.9(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=18955433; DOI=10.1101/gr.081901.108; RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.; RT "Ortho-proteogenomics: multiple proteomes investigation through orthology RT and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). RN [4] RP PROBABLE FUNCTION AS A KINASE WITH RSEA AS A SUBSTRATE, ACTIVITY RP REGULATION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x; RA Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.; RT "RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, RT is inactivated by phosphorylation-dependent ClpC1P2 proteolysis."; RL Mol. Microbiol. 75:592-606(2010). CC -!- FUNCTION: Protein kinase that regulates many aspects of mycobacterial CC physiology. Is a key component of a signal transduction pathway that CC regulates cell growth, cell shape and cell division via phosphorylation CC of target proteins (By similarity). Probably phosphorylates RseA CC (PubMed:20025669). {ECO:0000250|UniProtKB:P9WI81, CC ECO:0000305|PubMed:20025669}. 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 -!- ACTIVITY REGULATION: By K-252a. {ECO:0000305|PubMed:20025669}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- DOMAIN: The PASTA domains interact with peptidoglycans and are required CC for PknB localization. {ECO:0000250}. CC -!- PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity). CC {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: When depleted (with anti-sense RNA) no CC vancomycin-induced degradation of RseA is seen. CC {ECO:0000269|PubMed:20025669}. 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; CP000480; ABK74027.1; -; Genomic_DNA. DR EMBL; CP001663; AFP36514.1; -; Genomic_DNA. DR RefSeq; WP_003891355.1; NZ_SIJM01000001.1. DR RefSeq; YP_884449.1; NC_008596.1. DR AlphaFoldDB; A0QNG1; -. DR SMR; A0QNG1; -. DR STRING; 246196.MSMEG_0028; -. DR PaxDb; 246196-MSMEI_0031; -. DR GeneID; 66738220; -. DR KEGG; msg:MSMEI_0031; -. DR KEGG; msm:MSMEG_0028; -. DR PATRIC; fig|246196.19.peg.27; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000000757; Chromosome. DR Proteomes; UP000006158; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion 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:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt. DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt. 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; 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; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell membrane; Kinase; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..625 FT /note="Serine/threonine-protein kinase PknB" FT /id="PRO_0000422953" FT TOPO_DOM 1..331 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 332..352 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 353..625 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 11..274 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 355..421 FT /note="PASTA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 422..489 FT /note="PASTA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 490..556 FT /note="PASTA 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 557..625 FT /note="PASTA 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT REGION 302..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 591..612 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..612 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 93..95 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 140..143 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 143 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 156 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 169 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 171 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 294 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 295 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 309 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 625 AA; 66318 MW; E9B75950ADF718DA CRC64; MTTPQHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA QNAAALNHPA IVAVYDTGEA ETPNGPLPYI VMEYVDGVTL RDIVHTDGPI APRRAIEIIA DACQALNFSH QHGIIHRDVK PANIMISKNN AVKVMDFGIA RALADTGNSV TQTAAVIGTA QYLSPEQARG ETVDARSDVY SLGCVLYEIL TGEPPFIGDS PVAVAYQHVR EDPVPPSRRH ADVTPELDAV VLKALAKNPD NRYQTAAEMR ADLIRVHEGQ APDAPKVLTD AERTSMLAAP PADRAGAATQ DMPVPRPAGY SKQRSTSVAR WLIAVAVLAV LTVVVTVAIN MVGGNPRNVQ VPDVAEQSAD DAQAALQNRG FKTVIDRQPD NEVPPGLVIG TDPEAGSELG AGEQVTINVS TGPEQALVPD VAGLTPTQAR QKLKDAGFEK FRESPSPSTP EQKGRVLATN PQANQTAAII NEITIVVGAG PEDAPVLSCA GQNAESCKAI LAAGGFTNTV VVEVDNPAAA GQVVGTEPAD GQSVPKDTVI QIRVSKGNQF VMPDLVGQFW SDAYPRLTAL GWTGVLDKGP DVRDSGQRTN AVVTQSPSAG TPVNKDAKIT LSFAA //