PKNA_MYCTU
ID PKNA_MYCTU Reviewed; 431 AA.
AC P9WI83; L0T594; P65726; P71585;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Serine/threonine-protein kinase PknA;
DE EC=2.7.11.1;
GN Name=pknA; OrderedLocusNames=Rv0015c; ORFNames=MTCY10H4.15c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AUTOPHOSPHORYLATION,
RP OVEREXPRESSION, AND MUTAGENESIS OF LYS-42.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15985609; DOI=10.1101/gad.1311105;
RA Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C., Husson R.N.;
RT "The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB:
RT substrate identification and regulation of cell shape.";
RL Genes Dev. 19:1692-1704(2005).
RN [3]
RP FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, AND DEPHOSPHORYLATION BY PSTP.
RX PubMed=16817899; DOI=10.1111/j.1742-4658.2006.05289.x;
RA Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.;
RT "EmbR, a regulatory protein with ATPase activity, is a substrate of
RT multiple serine/threonine kinases and phosphatase in Mycobacterium
RT tuberculosis.";
RL FEBS J. 273:2711-2721(2006).
RN [4]
RP AUTOPHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16739134; DOI=10.1002/pmic.200500900;
RA Molle V., Zanella-Cleon I., Robin J.P., Mallejac S., Cozzone A.J.,
RA Becchi M.;
RT "Characterization of the phosphorylation sites of Mycobacterium
RT tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH
RT by mass spectrometry.";
RL Proteomics 6:3754-3766(2006).
RN [5]
RP FUNCTION AS A KINASE WITH GLMU AS SUBSTRATE.
RX PubMed=19121323; DOI=10.1016/j.jmb.2008.12.031;
RA Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K.;
RT "PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-
RT phosphate uridyltransferase, modulates its acetyltransferase activity.";
RL J. Mol. Biol. 386:451-464(2009).
RN [6]
RP FUNCTION AS A KINASE WITH WAG31 AS SUBSTRATE.
RX PubMed=21190553; DOI=10.1186/1471-2180-10-327;
RA Jani C., Eoh H., Lee J.J., Hamasha K., Sahana M.B., Han J.S.,
RA Nyayapathy S., Lee J.Y., Suh J.W., Lee S.H., Rehse S.J., Crick D.C.,
RA Kang C.M.;
RT "Regulation of polar peptidoglycan biosynthesis by Wag31 phosphorylation in
RT mycobacteria.";
RL BMC Microbiol. 10:327-327(2010).
RN [7]
RP RETRACTED PAPER.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066037; DOI=10.1371/journal.pone.0008590;
RA Sureka K., Hossain T., Mukherjee P., Chatterjee P., Datta P., Kundu M.,
RA Basu J.;
RT "Novel role of phosphorylation-dependent interaction between FtsZ and FipA
RT in mycobacterial cell division.";
RL PLoS ONE 5:E8590-E8590(2010).
RN [8]
RP RETRACTION NOTICE OF PUBMED:20066037.
RX PubMed=35202441; DOI=10.1371/journal.pone.0264672;
RG PLOS ONE Editors;
RL PLoS ONE 17:e0264672-e0264672(2022).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [10]
RP FUNCTION AS A KINASE WITH PSTP AS SUBSTRATE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21423706; DOI=10.1371/journal.pone.0017871;
RA Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y.;
RT "Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA
RT and PknB.";
RL PLoS ONE 6:E17871-E17871(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21829358; DOI=10.1371/journal.ppat.1002182;
RA Mir M., Asong J., Li X., Cardot J., Boons G.J., Husson R.N.;
RT "The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr
RT kinase PknB binds specific muropeptides and is required for PknB
RT localization.";
RL PLoS Pathog. 7:E1002182-E1002182(2011).
RN [12]
RP FUNCTION, IDENTIFICATION OF PRCA AND PRCB AS SUBSTRATE, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=H37Rv;
RX PubMed=25224505; DOI=10.1007/s12275-014-4416-2;
RA Anandan T., Han J., Baun H., Nyayapathy S., Brown J.T., Dial R.L.,
RA Moltalvo J.A., Kim M.S., Yang S.H., Ronning D.R., Husson R.N., Suh J.,
RA Kang C.M.;
RT "Phosphorylation regulates mycobacterial proteasome.";
RL J. Microbiol. 52:743-754(2014).
RN [13]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-42; THR-172;
RP THR-174 AND THR-180, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=25713147; DOI=10.1074/jbc.m114.611822;
RA Nagarajan S.N., Upadhyay S., Chawla Y., Khan S., Naz S., Subramanian J.,
RA Gandotra S., Nandicoori V.K.;
RT "Protein kinase A (PknA) of Mycobacterium tuberculosis is independently
RT activated and is critical for growth in vitro and survival of the pathogen
RT in the host.";
RL J. Biol. Chem. 290:9626-9645(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-283 IN AN INACTIVE STATE,
RP DOMAIN, PHOSPHORYLATION AT THR-172; THR-174 AND THR-180, ACTIVATION LOOP,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF 172-THR--THR-174 AND THR-180.
RX PubMed=25665034; DOI=10.1111/febs.13230;
RA Ravala S.K., Singh S., Yadav G.S., Kumar S., Karthikeyan S.,
RA Chakraborti P.K.;
RT "Evidence that phosphorylation of threonine in the GT motif triggers
RT activation of PknA, a eukaryotic-type serine/threonine kinase from
RT Mycobacterium tuberculosis.";
RL FEBS J. 282:1419-1431(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-336 IN AN INACTIVE STATE, AND
RP PHOSPHORYLATION AT THR-8; SER-10; THR-21; SER-46; THR-64; THR-65; SER-75;
RP THR-90; SER-105; THR-125; THR-152; THR-158; SER-198; THR-224; THR-252;
RP SER-263; THR-302; SER-309 AND THR-313.
RX PubMed=25586004; DOI=10.1002/prot.24754;
RA Wagner T., Alexandre M., Duran R., Barilone N., Wehenkel A., Alzari P.M.,
RA Bellinzoni M.;
RT "The crystal structure of the catalytic domain of the ser/thr kinase PknA
RT from M. tuberculosis shows an Src-like autoinhibited conformation.";
RL Proteins 83:982-988(2015).
CC -!- FUNCTION: Protein kinase that regulates many aspects of mycobacterial
CC physiology, and is critical for growth in vitro and survival of the
CC pathogen in the host (PubMed:25713147). Is a key component of a signal
CC transduction pathway that regulates cell growth, cell shape and cell
CC division via phosphorylation of target proteins such as FtsZ, Wag31,
CC GlmU, PstP, EmbR and Rv1422 (PubMed:15985609, PubMed:16817899,
CC PubMed:19121323, PubMed:21190553, PubMed:21423706). Also catalyzes the
CC phosphorylation of the proteasome alpha-subunit (PrcA) and unprocessed
CC proteasome beta-subunit (pre-PrcB), which results in the inhibition of
CC processing of pre-PrcB and assembly of the proteasome complex, and
CC thereby enhances the mycobacterial resistance to H(2)O(2); PknA thus
CC plays an important role in the oxidative stress response by impeding
CC the formation of holo-proteasome in M.tuberculosis under H(2)O(2)
CC stress (PubMed:25224505). Shows a strong preference for Thr versus Ser
CC as the phosphoacceptor. {ECO:0000269|PubMed:15985609,
CC ECO:0000269|PubMed:16817899, ECO:0000269|PubMed:19121323,
CC ECO:0000269|PubMed:21190553, ECO:0000269|PubMed:21423706,
CC ECO:0000269|PubMed:25224505, ECO:0000269|PubMed:25713147}.
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:15985609};
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:15985609};
CC -!- ACTIVITY REGULATION: Is activated by autophosphorylation of activation
CC loop threonine residues, which results in conformational change and
CC allows substrate binding. It seems that following ATP binding,
CC phosphate is first transferred to Thr-180 via a cis mechanism to
CC activate the kinase activity; phosphorylation of Thr-180 triggers PknA
CC to phosphorylate Thr-172/Thr-174 via a trans mechanism. Phosphorylation
CC of all of the activation loop threonines is necessary for efficient
CC catalytic activity. {ECO:0000269|PubMed:25665034}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21829358};
CC Single-pass membrane protein {ECO:0000269|PubMed:21829358}. Note=The
CC majority of the cells displays PknA expression at the membrane
CC perimeter along the length of the cell, whereas a minor population
CC shows PknA to localize at either or both poles (uni- and bipolar; 16
CC and 14%, respectively) and occasionally to both the poles and the
CC midcell (12%). {ECO:0000269|PubMed:25713147}.
CC -!- INDUCTION: Expressed predominantly in exponential phase.
CC {ECO:0000269|PubMed:15985609}.
CC -!- DOMAIN: The extracellular domain is dispensable for cell growth and
CC survival in vitro (PubMed:25713147). The catalytic activity of PknA is
CC confined within the N-terminal 283 amino acids (PubMed:25665034).
CC {ECO:0000269|PubMed:25665034, ECO:0000269|PubMed:25713147}.
CC -!- PTM: Autophosphorylated (PubMed:16739134) (PubMed:25665034)
CC (PubMed:25586004). Phosphorylation of Thr-180 in the activation loop is
CC critical for the functionality of PknA (PubMed:25665034).
CC Autophosphorylation level increases in the presence of H(2)O(2)
CC suggesting that PknA is activated by H(2)O(2) (PubMed:25224505).
CC Phosphorylation of the activation loop at Thr-172 of PknA is critical
CC for bacterial growth; PknA autophosphorylates its activation loop
CC independent of PknB (PubMed:25713147). Dephosphorylated by PstP
CC (PubMed:16817899). {ECO:0000269|PubMed:16739134,
CC ECO:0000269|PubMed:16817899, ECO:0000269|PubMed:25224505,
CC ECO:0000269|PubMed:25586004, ECO:0000269|PubMed:25665034,
CC ECO:0000269|PubMed:25713147}.
CC -!- DISRUPTION PHENOTYPE: PknA depletion in M.tuberculosis results in cell
CC death and aberrant cell morphology, and leads to complete clearance of
CC the pathogen from the host tissues using the murine infection model.
CC {ECO:0000269|PubMed:25713147}.
CC -!- MISCELLANEOUS: Overexpression causes major growth and morphological
CC changes that indicate defects in cell wall synthesis and possibly in
CC cell division. {ECO:0000305|PubMed:15985609}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: The article by Sureka et al was retracted by the editors after
CC publication. Concerns were raised regarding the results presented in
CC multiple figure panels. The raw data or replacement panels that were
CC available did not satisfactorily address all the issues, thus
CC questioning the integrity of the data. {ECO:0000305|PubMed:35202441}.
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DR EMBL; AL123456; CCP42737.1; -; Genomic_DNA.
DR PIR; E70699; E70699.
DR RefSeq; NP_214529.1; NC_000962.3.
DR RefSeq; WP_003400358.1; NZ_KK339370.1.
DR PDB; 4OW8; X-ray; 2.03 A; A=1-283.
DR PDB; 4X3F; X-ray; 2.90 A; A/B/C=1-336.
DR PDB; 6B2Q; X-ray; 2.88 A; A/B/C/D=1-296.
DR PDBsum; 4OW8; -.
DR PDBsum; 4X3F; -.
DR PDBsum; 6B2Q; -.
DR AlphaFoldDB; P9WI83; -.
DR SMR; P9WI83; -.
DR IntAct; P9WI83; 2.
DR STRING; 83332.Rv0015c; -.
DR BindingDB; P9WI83; -.
DR ChEMBL; CHEMBL4295585; -.
DR iPTMnet; P9WI83; -.
DR PaxDb; P9WI83; -.
DR DNASU; 885953; -.
DR GeneID; 45423974; -.
DR GeneID; 885953; -.
DR KEGG; mtu:Rv0015c; -.
DR TubercuList; Rv0015c; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; HYAGIVH; -.
DR PhylomeDB; P9WI83; -.
DR BRENDA; 2.7.11.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MTBBASE.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MTBBASE.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1990443; P:peptidyl-threonine autophosphorylation; IMP:CACAO.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:MTBBASE.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MTBBASE.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MTBBASE.
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 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..431
FT /note="Serine/threonine-protein kinase PknA"
FT /id="PRO_0000171205"
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 162..184
FT /note="Activation loop"
FT /evidence="ECO:0000305|PubMed:25665034"
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 MOD_RES 8
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 10
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 21
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 46
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 64
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 65
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 75
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 90
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 105
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 125
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 152
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 158
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 172
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25665034"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25665034"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25665034"
FT MOD_RES 198
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 224
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 252
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 263
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 302
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 309
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MOD_RES 313
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25586004"
FT MUTAGEN 42
FT /note="K->M: Loss of autophosphorylation activity. This
FT mutation results in cell death."
FT /evidence="ECO:0000269|PubMed:15985609,
FT ECO:0000269|PubMed:25713147"
FT MUTAGEN 172
FT /note="T->A: 10-fold reduction in transphosphorylation
FT activity. This mutant strain shows severely compromised
FT growth. Loss of autophosphorylation activity and weak
FT transphosphorylation activity; when associated with A-174."
FT /evidence="ECO:0000269|PubMed:25665034,
FT ECO:0000269|PubMed:25713147"
FT MUTAGEN 174
FT /note="T->A: 5-fold reduction in transphosphorylation
FT activity. Loss of autophosphorylation activity and weak
FT transphosphorylation activity; when associated with A-172."
FT /evidence="ECO:0000269|PubMed:25665034,
FT ECO:0000269|PubMed:25713147"
FT MUTAGEN 180
FT /note="T->A: Loss of auto- and transphosphorylation
FT activity."
FT /evidence="ECO:0000269|PubMed:25665034,
FT ECO:0000269|PubMed:25713147"
FT MUTAGEN 180
FT /note="T->E: Loss of transphosphorylation activity."
FT /evidence="ECO:0000269|PubMed:25713147"
FT MUTAGEN 180
FT /note="T->S: 4-fold reduction in transphosphorylation
FT activity."
FT /evidence="ECO:0000269|PubMed:25713147"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:4OW8"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4OW8"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4X3F"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4OW8"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4OW8"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6B2Q"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4OW8"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:4OW8"
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
