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 02-NOV-2016, entry version 62. 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 RT genomic analysis of Mycobacterium tuberculosis strain H37Ra versus RT H37Rv."; RL PLoS ONE 3:E2375-E2375(2008). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, RP AND 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 RT with 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, RP AUTOPHOSPHORYLATION, 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 RT kinase, to transphosphorylate MurD, a ligase involved in the process RT of 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 CC mycobacterial physiology. Is a key component of a signal CC transduction pathway that regulates cell growth, cell shape and CC cell division via phosphorylation of target proteins such as FtsZ CC and MurD. Shows a strong preference for Thr versus Ser as the CC phosphoacceptor. {ECO:0000269|PubMed:11856348, CC ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000269|PubMed:11856348, ECO:0000269|PubMed:17068335, CC ECO:0000269|PubMed:18557704}. CC -!- ENZYME REGULATION: Activated by magnesium or manganese. Inhibited CC by vanadate. {ECO:0000269|PubMed:11856348}. CC -!- SUBUNIT: Interacts with FtsZ and MurD. CC {ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass CC membrane protein {ECO:0000250}. CC -!- DOMAIN: The kinase domain and the juxtamembrane region contitute CC the catalytic core of PknA. Interaction between core and C- CC terminal domains is crucial for activity. CC {ECO:0000269|PubMed:18199749}. CC -!- PTM: Autophosphorylated. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {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; NC_009525.1. DR ProteinModelPortal; A5TY85; -. DR SMR; A5TY85; -. DR STRING; 419947.MtubH3_010100008962; -. DR PRIDE; A5TY85; -. DR EnsemblBacteria; ABQ71735; ABQ71735; MRA_0017. DR KEGG; mra:MRA_0017; -. DR PATRIC; 18139596; VBIMycTub106795_0021. DR eggNOG; ENOG4107TPY; Bacteria. DR eggNOG; COG0515; LUCA. DR HOGENOM; HOG000037187; -. DR KO; K12132; -. DR OMA; FVERFRI; -. DR Proteomes; UP000001988; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom. 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; SSF56112; 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; Complete proteome; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 431 Serine/threonine-protein kinase PknA. FT /FTId=PRO_0000419742. FT TOPO_DOM 1 339 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 340 360 Helical. {ECO:0000255}. FT TOPO_DOM 361 431 Extracellular. {ECO:0000255}. FT DOMAIN 13 272 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 19 27 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 141 141 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 42 42 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MUTAGEN 42 42 K->M: Lack of autophosphorylation. FT {ECO:0000269|PubMed:11856348, FT ECO:0000269|PubMed:18557704}. FT MUTAGEN 172 172 T->A: Strong decrease in FT autophosphorylation. FT {ECO:0000269|PubMed:18199749}. FT MUTAGEN 174 174 T->A: Decrease in autophosphorylation. FT {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 //