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Serine/threonine-protein kinase PknB (EC 2.7.11.1)

 PKNB_MYCTU              Reviewed;         626 AA.
P9WI81; L0T5F6; P0A5S4; P71584;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 35.
RecName: Full=Serine/threonine-protein kinase PknB;
EC=2.7.11.1;
Name=pknB; OrderedLocusNames=Rv0014c; ORFNames=MTCY10H4.14c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
PROTEIN SEQUENCE OF 162-189, CATALYTIC ACTIVITY, PHOSPHORYLATION AT
THR-171 AND THR-173, MUTAGENESIS OF THR-171 AND THR-173, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12950916; DOI=10.1046/j.1365-2958.2003.03657.x;
Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T.,
Cervenansky C., Alzari P.M.;
"PknB kinase activity is regulated by phosphorylation in two Thr
residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr
phosphatase, in Mycobacterium tuberculosis.";
Mol. Microbiol. 49:1493-1508(2003).
[3]
CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10531215;
Av-Gay Y., Jamil S., Drews S.J.;
"Expression and characterization of the Mycobacterium tuberculosis
serine/threonine protein kinase PknB.";
Infect. Immun. 67:5676-5682(1999).
[4]
PHOSPHORYLATION AT SER-166; THR-171; THR-173; THR-294 AND THR-309, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15967413; DOI=10.1016/j.bbrc.2005.05.173;
Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P.,
Boitel B., Cole S.T., Alzari P.M., Cervenansky C.;
"Conserved autophosphorylation pattern in activation loops and
juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein
kinases.";
Biochem. Biophys. Res. Commun. 333:858-867(2005).
[5]
FUNCTION, CATALYTIC ACTIVITY, INDUCTION, PHOSPHORYLATION AT THR-171
AND THR-173, OVEREXPRESSION, AND MUTAGENESIS OF LYS-40.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15985609; DOI=10.1101/gad.1311105;
Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C.,
Husson R.N.;
"The Mycobacterium tuberculosis serine/threonine kinases PknA and
PknB: substrate identification and regulation of cell shape.";
Genes Dev. 19:1692-1704(2005).
[6]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GARA, AND MUTAGENESIS
OF THR-171 AND THR-173.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15978616; DOI=10.1016/j.jmb.2005.05.049;
Villarino A., Duran R., Wehenkel A., Fernandez P., England P.,
Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C.,
Alzari P.M.;
"Proteomic identification of M. tuberculosis protein kinase
substrates: PknB recruits GarA, a FHA domain-containing protein,
through activation loop-mediated interactions.";
J. Mol. Biol. 350:953-963(2005).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15987910; DOI=10.1110/ps.051413405;
Grundner C., Gay L.M., Alber T.;
"Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE,
and PknF phosphorylate multiple FHA domains.";
Protein Sci. 14:1918-1921(2005).
[8]
FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, AND DEPHOSPHORYLATION BY
PSTP.
PubMed=16817899; DOI=10.1111/j.1742-4658.2006.05289.x;
Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.;
"EmbR, a regulatory protein with ATPase activity, is a substrate of
multiple serine/threonine kinases and phosphatase in Mycobacterium
tuberculosis.";
FEBS J. 273:2711-2721(2006).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16980473; DOI=10.1128/JB.00963-06;
Fernandez P., Saint-Joanis B., Barilone N., Jackson M., Gicquel B.,
Cole S.T., Alzari P.M.;
"The Ser/Thr protein kinase PknB is essential for sustaining
mycobacterial growth.";
J. Bacteriol. 188:7778-7784(2006).
[10]
FUNCTION AS A KINASE WITH PBPA AS SUBSTRATE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16436437; DOI=10.1099/mic.0.28630-0;
Dasgupta A., Datta P., Kundu M., Basu J.;
"The serine/threonine kinase PknB of Mycobacterium tuberculosis
phosphorylates PBPA, a penicillin-binding protein required for cell
division.";
Microbiology 152:493-504(2006).
[11]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FHAB, AND MUTAGENESIS
OF LYS-40; THR-171; THR-173; THR-294 AND THR-309.
PubMed=19826007; DOI=10.1074/jbc.M109.058834;
Gupta M., Sajid A., Arora G., Tandon V., Singh Y.;
"Forkhead-associated domain-containing protein Rv0019c and polyketide-
associated protein PapA5, from substrates of serine/threonine protein
kinase PknB to interacting proteins of Mycobacterium tuberculosis.";
J. Biol. Chem. 284:34723-34734(2009).
[12]
FUNCTION AS A KINASE WITH GLMU AS SUBSTRATE.
PubMed=19121323; DOI=10.1016/j.jmb.2008.12.031;
Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K.;
"PknB-mediated phosphorylation of a novel substrate, N-
acetylglucosamine-1-phosphate uridyltransferase, modulates its
acetyltransferase activity.";
J. Mol. Biol. 386:451-464(2009).
[13]
FUNCTION AS A KINASE WITH RSEA AS A SUBSTRATE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
"RseA, the SigE specific anti-sigma factor of Mycobacterium
tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2
proteolysis.";
Mol. Microbiol. 75:592-606(2010).
[14]
ENZYME REGULATION, SUBUNIT, AND MUTAGENESIS OF ARG-10; LEU-33; ASP-76
AND ASP-138.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21134645; DOI=10.1016/j.str.2010.09.019;
Lombana T.N., Echols N., Good M.C., Thomsen N.D., Ng H.L.,
Greenstein A.E., Falick A.M., King D.S., Alber T.;
"Allosteric activation mechanism of the Mycobacterium tuberculosis
receptor Ser/Thr protein kinase, PknB.";
Structure 18:1667-1677(2010).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[16]
FUNCTION AS A KINASE WITH PSTP AS SUBSTRATE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21423706; DOI=10.1371/journal.pone.0017871;
Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y.;
"Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by
PknA and PknB.";
PLoS ONE 6:E17871-E17871(2011).
[17]
ENZYME REGULATION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=21829358; DOI=10.1371/journal.ppat.1002182;
Mir M., Asong J., Li X., Cardot J., Boons G.J., Husson R.N.;
"The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr
kinase PknB binds specific muropeptides and is required for PknB
localization.";
PLoS Pathog. 7:E1002182-E1002182(2011).
[18]
INTERACTION WITH FHAA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22000520; DOI=10.1016/j.str.2011.07.011;
Roumestand C., Leiba J., Galophe N., Margeat E., Padilla A.,
Bessin Y., Barthe P., Molle V., Cohen-Gonsaud M.;
"Structural insight into the Mycobacterium tuberculosis Rv0020c
protein and its interaction with the PknB kinase.";
Structure 19:1525-1534(2011).
[19]
FUNCTION.
PubMed=22275220; DOI=10.1126/scisignal.2002525;
Gee C.L., Papavinasasundaram K.G., Blair S.R., Baer C.E., Falick A.M.,
King D.S., Griffin J.E., Venghatakrishnan H., Zukauskas A., Wei J.R.,
Dhiman R.K., Crick D.C., Rubin E.J., Sassetti C.M., Alber T.;
"A phosphorylated pseudokinase complex controls cell wall synthesis in
mycobacteria.";
Sci. Signal. 5:RA7-RA7(2012).
[20]
FUNCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
STRAIN=H37Rv;
PubMed=24706757; DOI=10.1074/jbc.M114.563536;
Chawla Y., Upadhyay S., Khan S., Nagarajan S.N., Forti F.,
Nandicoori V.K.;
"Protein kinase B (PknB) of Mycobacterium tuberculosis is essential
for growth of the pathogen in vitro as well as for survival within the
host.";
J. Biol. Chem. 289:13858-13875(2014).
[21]
FUNCTION, AND IDENTIFICATION OF PRCA AS SUBSTRATE.
STRAIN=H37Rv;
PubMed=25224505; DOI=10.1007/s12275-014-4416-2;
Anandan T., Han J., Baun H., Nyayapathy S., Brown J.T., Dial R.L.,
Moltalvo J.A., Kim M.S., Yang S.H., Ronning D.R., Husson R.N., Suh J.,
Kang C.M.;
"Phosphorylation regulates mycobacterial proteasome.";
J. Microbiol. 52:743-754(2014).
[22]
FUNCTION, AND INDUCTION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=24409094; DOI=10.1371/journal.pbio.1001746;
Ortega C., Liao R., Anderson L.N., Rustad T., Ollodart A.R.,
Wright A.T., Sherman D.R., Grundner C.;
"Mycobacterium tuberculosis Ser/Thr protein kinase B mediates an
oxygen-dependent replication switch.";
PLoS Biol. 12:E1001746-E1001746(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-279 IN COMPLEX WITH ATP.
PubMed=12551895; DOI=10.1074/jbc.M300660200;
Ortiz-Lombardia M., Pompeo F., Boitel B., Alzari P.M.;
"Crystal structure of the catalytic domain of the PknB
serine/threonine kinase from Mycobacterium tuberculosis.";
J. Biol. Chem. 278:13094-13100(2003).
[24]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-308 IN COMPLEX WITH ATP,
CATALYTIC ACTIVITY, METAL BINDING AT ASN-143 AND ASP-156, ATP BINDING
AT LYS-40, PHOSPHORYLATION AT SER-166; SER-169; THR-171; THR-173;
THR-294 AND SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12548283; DOI=10.1038/nsb897;
Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., Alber T.;
"Structure of Mycobacterium tuberculosis PknB supports a universal
activation mechanism for Ser/Thr protein kinases.";
Nat. Struct. Biol. 10:168-174(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 1-279 IN COMPLEX WITH
MITOXANTRONE, ENZYME REGULATION, AND SUBUNIT.
PubMed=16674948; DOI=10.1016/j.febslet.2006.04.046;
Wehenkel A., Fernandez P., Bellinzoni M., Catherinot V., Barilone N.,
Labesse G., Jackson M., Alzari P.M.;
"The structure of PknB in complex with mitoxantrone, an ATP-
competitive inhibitor, suggests a mode of protein kinase regulation in
mycobacteria.";
FEBS Lett. 580:3018-3022(2006).
[26]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-308 IN COMPLEX WITH ADP,
AND PHOSPHORYLATION AT THR-171.
PubMed=19008858; DOI=10.1038/emboj.2008.236;
Mieczkowski C., Iavarone A.T., Alber T.;
"Auto-activation mechanism of the Mycobacterium tuberculosis PknB
receptor Ser/Thr kinase.";
EMBO J. 27:3186-3197(2008).
[27]
STRUCTURE BY NMR OF 355-491, AND ENZYME REGULATION.
PubMed=20462494; DOI=10.1016/j.str.2010.02.013;
Barthe P., Mukamolova G.V., Roumestand C., Cohen-Gonsaud M.;
"The structure of PknB extracellular PASTA domain from mycobacterium
tuberculosis suggests a ligand-dependent kinase activation.";
Structure 18:606-615(2010).
-!- FUNCTION: Protein kinase that regulates many aspects of
mycobacterial physiology, and is critical for growth in vitro and
survival of the pathogen in the host (PubMed:24706757). Is a key
component of a signal transduction pathway that regulates cell
growth, cell shape and cell division via phosphorylation of target
proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA
(Rv0020c), MviN, PstP, EmbR, Rv1422, Rv1747 and RseA
(PubMed:15978616, PubMed:15985609, PubMed:15987910,
PubMed:16436437, PubMed:16817899, PubMed:16980473,
PubMed:19121323, PubMed:19826007, PubMed:20025669,
PubMed:21423706, PubMed:22275220). Also catalyzes the
phosphorylation of the core proteasome alpha-subunit (PrcA), and
thereby regulates the proteolytic activity of the proteasome
(PubMed:25224505). Is a major regulator of the oxygen-dependent
replication switch since PknB activity is necessary for
reactivation of cells from the hypoxic state (PubMed:24409094).
Shows a strong preference for Thr versus Ser as the
phosphoacceptor. Overexpression of PknB alters cell morphology and
leads to cell death (PubMed:24706757) (PubMed:24409094).
{ECO:0000269|PubMed:15978616, ECO:0000269|PubMed:15985609,
ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:16436437,
ECO:0000269|PubMed:16817899, ECO:0000269|PubMed:16980473,
ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19826007,
ECO:0000269|PubMed:20025669, ECO:0000269|PubMed:21423706,
ECO:0000269|PubMed:22275220, ECO:0000269|PubMed:24409094,
ECO:0000269|PubMed:24706757, ECO:0000269|PubMed:25224505}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10531215, ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15978616,
ECO:0000269|PubMed:15985609, ECO:0000269|PubMed:15987910,
ECO:0000269|PubMed:19826007}.
-!- ENZYME REGULATION: Interaction of the PASTA domains with
peptidoglycan leads to septal and polar localization of PknB, and
dimerization of the intracellular kinase domain. Dimerization
activates the kinase domain via an allosteric mechanism,
triggering autophosphorylation and phosphorylation of target
proteins. Inhibited by mitoxantrone. Inhibition prevents
mycobacterial growth. {ECO:0000269|PubMed:16674948,
ECO:0000269|PubMed:20462494, ECO:0000269|PubMed:21134645,
ECO:0000269|PubMed:21829358}.
-!- SUBUNIT: Homodimer. Interacts with the FHA domain of GarA, FhaB
and FhaA. {ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895, ECO:0000269|PubMed:15978616,
ECO:0000269|PubMed:16674948, ECO:0000269|PubMed:19008858,
ECO:0000269|PubMed:19826007, ECO:0000269|PubMed:21134645,
ECO:0000269|PubMed:22000520}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-2946037, EBI-2946037;
P71590:fhaA; NbExp=4; IntAct=EBI-2946037, EBI-15896562;
P9WJA9:garA; NbExp=2; IntAct=EBI-2946037, EBI-6405522;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21829358};
Single-pass membrane protein {ECO:0000269|PubMed:21829358}.
Note=Localizes to septum and cell poles (PubMed:21829358). The
localization of PknB to the cell membrane is essential for cell
survival (PubMed:24706757). {ECO:0000269|PubMed:21829358,
ECO:0000269|PubMed:24706757}.
-!- INDUCTION: Expressed predominantly in exponential phase
(PubMed:15985609). PknB levels are regulated in response to
hypoxia; its expression is down-regulated during hypoxia and
recovers to aerated levels upon reaeration (at mRNA and protein
level) (PubMed:24409094). {ECO:0000269|PubMed:15985609,
ECO:0000269|PubMed:24409094}.
-!- DOMAIN: The intracellular kinase domain and all four
extracytoplasmic PASTA domains are essential for PknB function and
cell survival (PubMed:24706757). The PASTA domains interact with
peptidoglycans and are required for PknB localization
(PubMed:21829358). {ECO:0000269|PubMed:21829358,
ECO:0000269|PubMed:24706757}.
-!- PTM: Autophosphorylated. Dephosphorylated by PstP.
{ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609,
ECO:0000269|PubMed:19008858}.
-!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted
(PubMed:16980473). PknB depletion in M.tuberculosis results in
cell death and aberrant cell morphology, and leads to complete
clearance of the pathogen from the host tissues using the murine
infection model (PubMed:24706757). {ECO:0000269|PubMed:16980473,
ECO:0000269|PubMed:24706757}.
-!- MISCELLANEOUS: Overexpression causes major growth and
morphological changes that indicate defects in cell wall synthesis
and possibly in cell division. {ECO:0000305|PubMed:15985609}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; AL123456; CCP42736.1; -; Genomic_DNA.
PIR; D70699; D70699.
RefSeq; NP_214528.1; NC_000962.3.
RefSeq; WP_003400356.1; NZ_KK339370.1.
PDB; 1MRU; X-ray; 3.00 A; A/B=1-308.
PDB; 1O6Y; X-ray; 2.20 A; A=1-279.
PDB; 2FUM; X-ray; 2.89 A; A/B/C/D=1-279.
PDB; 2KUD; NMR; -; A=355-491.
PDB; 2KUE; NMR; -; A=423-557.
PDB; 2KUF; NMR; -; A=491-626.
PDB; 2KUI; NMR; -; A=355-626.
PDB; 3F61; X-ray; 1.80 A; A=1-308.
PDB; 3F69; X-ray; 2.80 A; A/B=1-308.
PDB; 3ORI; X-ray; 2.00 A; A/B/C/D=1-308.
PDB; 3ORO; X-ray; 1.90 A; A=1-308.
PDB; 5E0Y; X-ray; 2.00 A; A=558-626.
PDB; 5E0Z; X-ray; 2.00 A; A=491-626.
PDB; 5E10; X-ray; 1.80 A; A=360-491.
PDB; 5E12; X-ray; 2.21 A; A/B=423-626.
PDB; 5U94; X-ray; 2.20 A; A=1-280.
PDBsum; 1MRU; -.
PDBsum; 1O6Y; -.
PDBsum; 2FUM; -.
PDBsum; 2KUD; -.
PDBsum; 2KUE; -.
PDBsum; 2KUF; -.
PDBsum; 2KUI; -.
PDBsum; 3F61; -.
PDBsum; 3F69; -.
PDBsum; 3ORI; -.
PDBsum; 3ORO; -.
PDBsum; 5E0Y; -.
PDBsum; 5E0Z; -.
PDBsum; 5E10; -.
PDBsum; 5E12; -.
PDBsum; 5U94; -.
ProteinModelPortal; P9WI81; -.
SMR; P9WI81; -.
IntAct; P9WI81; 4.
MINT; P9WI81; -.
STRING; 83332.Rv0014c; -.
BindingDB; P9WI81; -.
ChEMBL; CHEMBL1908385; -.
iPTMnet; P9WI81; -.
PaxDb; P9WI81; -.
EnsemblBacteria; CCP42736; CCP42736; Rv0014c.
GeneID; 887072; -.
KEGG; mtu:Rv0014c; -.
TubercuList; Rv0014c; -.
eggNOG; ENOG4105D9P; Bacteria.
eggNOG; COG0515; LUCA.
eggNOG; COG2815; LUCA.
KO; K12132; -.
OMA; ICAKAMA; -.
PhylomeDB; P9WI81; -.
PRO; PR:P9WI81; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MTBBASE.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MTBBASE.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:MTBBASE.
GO; GO:0032091; P:negative regulation of protein binding; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:MTBBASE.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:MTBBASE.
GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
GO; GO:0008360; P:regulation of cell shape; IMP:MTBBASE.
GO; GO:0052572; P:response to host immune response; IDA:MTBBASE.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR005543; PASTA_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03793; PASTA; 4.
Pfam; PF00069; Pkinase; 1.
SMART; SM00740; PASTA; 4.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51178; PASTA; 4.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane;
Complete proteome; Direct protein sequencing; Kinase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Transmembrane; Transmembrane helix; Virulence.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 626 Serine/threonine-protein kinase PknB.
/FTId=PRO_0000171208.
TOPO_DOM 2 332 Cytoplasmic. {ECO:0000255}.
TRANSMEM 333 353 Helical. {ECO:0000255}.
TOPO_DOM 354 626 Extracellular. {ECO:0000255}.
DOMAIN 11 274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 356 422 PASTA 1. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 423 490 PASTA 2. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 491 557 PASTA 3. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 558 626 PASTA 4. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
NP_BIND 17 25 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895}.
NP_BIND 93 95 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895}.
NP_BIND 140 143 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895}.
ACT_SITE 138 138 Proton acceptor.
METAL 143 143 Magnesium.
METAL 156 156 Magnesium.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895}.
BINDING 156 156 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12551895}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:21969609}.
MOD_RES 166 166 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:15967413}.
MOD_RES 169 169 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12548283}.
MOD_RES 171 171 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:15967413,
ECO:0000269|PubMed:15985609,
ECO:0000269|PubMed:19008858}.
MOD_RES 173 173 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:15967413,
ECO:0000269|PubMed:15985609}.
MOD_RES 294 294 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12548283,
ECO:0000269|PubMed:15967413}.
MOD_RES 295 295 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12548283}.
MOD_RES 309 309 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:15967413}.
MUTAGEN 10 10 R->A: Impairs kinase activity.
{ECO:0000269|PubMed:21134645}.
MUTAGEN 33 33 L->D: Impairs kinase activity.
{ECO:0000269|PubMed:21134645}.
MUTAGEN 40 40 K->M: Lack of autophosphorylation.
Decreases affinity for FhaB.
{ECO:0000269|PubMed:15985609,
ECO:0000269|PubMed:19826007}.
MUTAGEN 76 76 D->A: Impairs kinase activity.
{ECO:0000269|PubMed:21134645}.
MUTAGEN 138 138 D->N: Impairs kinase activity.
{ECO:0000269|PubMed:21134645}.
MUTAGEN 171 171 T->A: Reduces activity and
autophosphorylation. Decreases
interaction with GarA.
{ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:15978616,
ECO:0000269|PubMed:19826007}.
MUTAGEN 173 173 T->A: Reduces activity and
autophosphorylation. Decreases
interaction with GarA.
{ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:15978616,
ECO:0000269|PubMed:19826007}.
MUTAGEN 294 294 T->A: Does not affect activity.
{ECO:0000269|PubMed:19826007}.
MUTAGEN 309 309 T->A: Does not affect activity.
{ECO:0000269|PubMed:19826007}.
STRAND 5 7 {ECO:0000244|PDB:3F61}.
TURN 8 10 {ECO:0000244|PDB:3F61}.
STRAND 11 19 {ECO:0000244|PDB:3F61}.
STRAND 21 30 {ECO:0000244|PDB:3F61}.
TURN 31 34 {ECO:0000244|PDB:3F61}.
STRAND 35 42 {ECO:0000244|PDB:3F61}.
HELIX 44 46 {ECO:0000244|PDB:3F61}.
HELIX 50 60 {ECO:0000244|PDB:3F61}.
STRAND 74 82 {ECO:0000244|PDB:3F61}.
STRAND 85 93 {ECO:0000244|PDB:3F61}.
STRAND 97 99 {ECO:0000244|PDB:3F61}.
HELIX 100 107 {ECO:0000244|PDB:3F61}.
HELIX 112 131 {ECO:0000244|PDB:3F61}.
HELIX 141 143 {ECO:0000244|PDB:3F61}.
STRAND 144 147 {ECO:0000244|PDB:3F61}.
STRAND 152 154 {ECO:0000244|PDB:3F61}.
STRAND 167 169 {ECO:0000244|PDB:3F69}.
STRAND 176 179 {ECO:0000244|PDB:3ORO}.
HELIX 180 182 {ECO:0000244|PDB:5U94}.
HELIX 185 189 {ECO:0000244|PDB:3F61}.
HELIX 195 211 {ECO:0000244|PDB:3F61}.
HELIX 221 230 {ECO:0000244|PDB:3F61}.
HELIX 236 239 {ECO:0000244|PDB:3F61}.
STRAND 240 242 {ECO:0000244|PDB:1O6Y}.
HELIX 245 254 {ECO:0000244|PDB:3F61}.
HELIX 259 261 {ECO:0000244|PDB:3F61}.
HELIX 266 277 {ECO:0000244|PDB:3F61}.
STRAND 358 361 {ECO:0000244|PDB:2KUI}.
HELIX 370 379 {ECO:0000244|PDB:5E10}.
STRAND 383 389 {ECO:0000244|PDB:5E10}.
STRAND 392 394 {ECO:0000244|PDB:5E10}.
STRAND 398 404 {ECO:0000244|PDB:5E10}.
STRAND 408 410 {ECO:0000244|PDB:2KUI}.
STRAND 415 421 {ECO:0000244|PDB:5E10}.
STRAND 426 428 {ECO:0000244|PDB:5E10}.
HELIX 433 435 {ECO:0000244|PDB:2KUD}.
HELIX 437 446 {ECO:0000244|PDB:5E10}.
STRAND 452 458 {ECO:0000244|PDB:5E10}.
HELIX 461 463 {ECO:0000244|PDB:5E10}.
STRAND 466 472 {ECO:0000244|PDB:5E10}.
STRAND 477 479 {ECO:0000244|PDB:5E10}.
STRAND 484 490 {ECO:0000244|PDB:5E10}.
STRAND 494 496 {ECO:0000244|PDB:5E0Z}.
STRAND 502 504 {ECO:0000244|PDB:2KUF}.
HELIX 505 515 {ECO:0000244|PDB:5E0Z}.
STRAND 520 525 {ECO:0000244|PDB:5E0Z}.
STRAND 533 539 {ECO:0000244|PDB:5E0Z}.
STRAND 544 546 {ECO:0000244|PDB:5E0Z}.
STRAND 551 556 {ECO:0000244|PDB:5E0Z}.
STRAND 560 562 {ECO:0000244|PDB:5E0Z}.
HELIX 571 579 {ECO:0000244|PDB:5E0Z}.
TURN 580 582 {ECO:0000244|PDB:5E0Z}.
STRAND 587 589 {ECO:0000244|PDB:5E0Z}.
HELIX 597 599 {ECO:0000244|PDB:5E0Z}.
STRAND 602 608 {ECO:0000244|PDB:5E0Z}.
STRAND 613 615 {ECO:0000244|PDB:5E0Z}.
STRAND 620 625 {ECO:0000244|PDB:5E0Z}.
SEQUENCE 626 AA; 66510 MW; 6C27EEBE9D5A453B CRC64;
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL RDIVHTEGPM TPKRAIEVIA
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSGNSV TQTAAVIGTA
QYLSPEQARG DSVDARSDVY SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH
EGLSADLDAV VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI NTFGGITRDV
QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI GTDPAANTSV SAGDEITVNV
STGPEQREIP DVSTLTYAEA VKKLTAAGFG RFKQANSPST PELVGKVIGT NPPANQTSAI
TNVVIIIVGS GPATKDIPDV AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP
AGTTVPVDSV IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH
NRVVYQNPPA GTGVNRDGII TLRFGQ


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