PKNA_MYCTA
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 03-AUG-2022, entry version 85.
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}.
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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: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: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; 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; 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
