ID PKNA_MYCTA Reviewed; 431 AA. AC A5TY85; DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-DEC-2022, entry version 86. DE RecName: Full=Serine/threonine-protein kinase PknA; DE EC=2.7.11.1; GN Name=pknA; OrderedLocusNames=MRA_0017; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra; RX PubMed=18584054; DOI=10.1371/journal.pone.0002375; RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L., RA Wang H., Wang S., Zhao G., Zhang Y.; RT "Genetic basis of virulence attenuation revealed by comparative genomic RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv."; RL PLoS ONE 3:E2375-E2375(2008). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AUTOPHOSPHORYLATION, AND RP MUTAGENESIS OF LYS-42. RC STRAIN=ATCC 25177 / H37Ra; RX PubMed=11856348; DOI=10.1046/j.1432-1033.2002.02778.x; RA Chaba R., Raje M., Chakraborti P.K.; RT "Evidence that a eukaryotic-type serine/threonine protein kinase from RT Mycobacterium tuberculosis regulates morphological changes associated with RT cell division."; RL Eur. J. Biochem. 269:1078-1085(2002). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH FTSZ. RC STRAIN=ATCC 25177 / H37Ra; RX PubMed=17068335; DOI=10.1074/jbc.m607216200; RA Thakur M., Chakraborti P.K.; RT "GTPase activity of mycobacterial FtsZ is impaired due to its RT transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA."; RL J. Biol. Chem. 281:40107-40113(2006). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MURD, AUTOPHOSPHORYLATION, RP AND MUTAGENESIS OF LYS-42. RC STRAIN=ATCC 25177 / H37Ra; RX PubMed=18557704; DOI=10.1042/bj20080234; RA Thakur M., Chakraborti P.K.; RT "Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, RT to transphosphorylate MurD, a ligase involved in the process of RT peptidoglycan biosynthesis."; RL Biochem. J. 415:27-33(2008). RN [5] RP AUTOPHOSPHORYLATION, DOMAIN, AND MUTAGENESIS OF THR-172 AND THR-174. RC STRAIN=ATCC 25177 / H37Ra; RX PubMed=18199749; DOI=10.1074/jbc.m707535200; RA Thakur M., Chaba R., Mondal A.K., Chakraborti P.K.; RT "Interdomain interaction reconstitutes the functionality of PknA, a RT eukaryotic type Ser/Thr kinase from Mycobacterium tuberculosis."; RL J. Biol. Chem. 283:8023-8033(2008). 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 such as FtsZ and MurD. Shows a strong preference for CC Thr versus Ser as the phosphoacceptor. {ECO:0000269|PubMed:11856348, CC ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}. 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:0000269|PubMed:11856348, ECO:0000269|PubMed:17068335, CC ECO:0000269|PubMed:18557704}; 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:0000269|PubMed:11856348, CC ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}; CC -!- ACTIVITY REGULATION: Activated by magnesium or manganese. Inhibited by CC vanadate. {ECO:0000269|PubMed:11856348}. CC -!- SUBUNIT: Interacts with FtsZ and MurD. {ECO:0000269|PubMed:17068335, CC ECO:0000269|PubMed:18557704}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane CC protein {ECO:0000250}. CC -!- DOMAIN: The kinase domain and the juxtamembrane region constitute the CC catalytic core of PknA. Interaction between core and C-terminal domains CC is crucial for activity. {ECO:0000269|PubMed:18199749}. CC -!- PTM: Autophosphorylated. 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; CP000611; ABQ71735.1; -; Genomic_DNA. DR RefSeq; WP_003400358.1; NZ_CP016972.1. DR AlphaFoldDB; A5TY85; -. DR SMR; A5TY85; -. DR STRING; 419947.MRA_0017; -. DR EnsemblBacteria; ABQ71735; ABQ71735; MRA_0017. DR GeneID; 45423974; -. DR KEGG; mra:MRA_0017; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR OMA; HYAGIVH; -. DR OrthoDB; 1377603at2; -. DR Proteomes; UP000001988; 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:0006468; P:protein phosphorylation; IEA:InterPro. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. 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 1: Evidence at protein level; KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Serine/threonine-protein kinase; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..431 FT /note="Serine/threonine-protein kinase PknA" FT /id="PRO_0000419742" FT TOPO_DOM 1..339 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 361..431 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 13..272 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 276..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 366..418 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..316 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 366..394 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..417 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 141 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 19..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MUTAGEN 42 FT /note="K->M: Lack of autophosphorylation." FT /evidence="ECO:0000269|PubMed:11856348, FT ECO:0000269|PubMed:18557704" FT MUTAGEN 172 FT /note="T->A: Strong decrease in autophosphorylation." FT /evidence="ECO:0000269|PubMed:18199749" FT MUTAGEN 174 FT /note="T->A: Decrease in autophosphorylation." FT /evidence="ECO:0000269|PubMed:18199749" SQ SEQUENCE 431 AA; 45597 MW; 582D183747F3C111 CRC64; MSPRVGVTLS GRYRLQRLIA TGGMGQVWEA VDNRLGRRVA VKVLKSEFSS DPEFIERFRA EARTTAMLNH PGIASVHDYG ESQMNGEGRT AYLVMELVNG EPLNSVLKRT GRLSLRHALD MLEQTGRALQ IAHAAGLVHR DVKPGNILIT PTGQVKITDF GIAKAVDAAP VTQTGMVMGT AQYIAPEQAL GHDASPASDV YSLGVVGYEA VSGKRPFAGD GALTVAMKHI KEPPPPLPPD LPPNVRELIE ITLVKNPAMR YRSGGPFADA VAAVRAGRRP PRPSQTPPPG RAAPAAIPSG TTARVAANSA GRTAASRRSR PATGGHRPPR RTFSSGQRAL LWAAGVLGAL AIIIAVLLVI KAPGDNSPQQ APTPTVTTTG NPPASNTGGT DASPRLNWTE RGETRHSGLQ SWVVPPTPHS RASLARYEIA Q //