ID   PKNG_MYCLE              Reviewed;         763 AA.
AC   P57993; Q9ZBL8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Serine/threonine-protein kinase PknG;
DE            EC=2.7.11.1;
GN   Name=pknG; OrderedLocusNames=ML0304; ORFNames=MLCB1450.19c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- 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;
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC29812.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL035159; CAA22703.1; -; Genomic_DNA.
DR   EMBL; AL583918; CAC29812.1; ALT_INIT; Genomic_DNA.
DR   PIR; H86946; H86946.
DR   PIR; T44735; T44735.
DR   AlphaFoldDB; P57993; -.
DR   SMR; P57993; -.
DR   STRING; 272631.gene:17574123; -.
DR   KEGG; mle:ML0304; -.
DR   Leproma; ML0304; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   Proteomes; UP000000806; Chromosome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..763
FT                   /note="Serine/threonine-protein kinase PknG"
FT                   /id="PRO_0000171215"
FT   DOMAIN          160..406
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         166..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   763 AA;  83470 MW;  9B42725EB49C1199 CRC64;
     MKREHMDHDT EDVGQAAQRA DPPSGTTEGR LQSTQAIFRP NFDDDDDLLH ISVPSVDTEP
     QDRITPATRV LPPIRQLGGG LVEIRRVRDI DPLEALMTNP VVPESKRFCW NCGRPVGRSE
     LEGQEADGAQ GAKEGWCPYC GSPYSFLPQL SPGDIVAGQY EVKGCIAHGG LGWVYLAFDH
     NVNDRPVVLK GLVHSGDAEA QASAVAERQF LAEVVHPQIV QIFNFVEHKD TSGDPVGYIV
     MEYIGGRSLK RGSKKGNVEK LPVAEAIAYL LEILPALSYL HSIGLVYNDL KPENIMLTEE
     QLKLIDLGAV SRINSFGCIY GTPGYQAPEI VRTGPTVATD IYTVGRTLAA LTLNLRTRNG
     RYMDGLPEDD PVLTTYDSFA RLLHRAINPD PRRRFSSAEE MSAQLMGVLR EVVAQDTGVP
     RAGLSTIFSP SRSTFGVDLL VAHTDVYLDG RLHSEKLTAK DIVTALQVPL VDPTDVAAPV
     LQATVLSQPV QTLDSLRAAR HGMLDAQGID LAESVELPLM EVRALLDLGD VVKANRKLDD
     LADRVSCQWR LVWYRAVADL LTGDYASATK HFTEVLNTFP GELAPKLALA ATAELAGESD
     EHKFYRTVWH TNDGVVSAAF GLARFQSAEG DRTGAVCTLD EVPPTSRHFT TARLTSAVTL
     LSGRSTNEIT EQQIRDAARR VETLPPTEPR VLQIRALVLG CAMDWLADNQ ASANHILGFP
     FTKHGLRLGV EASLRSLARV APTQRHRYTL VDMANKVRPT STL
//