PKNG_MYCLE
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 03-AUG-2022, entry version 116.
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; Actinobacteria; Corynebacteriales; 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 RefSeq; WP_010907662.1; NC_002677.1.
DR AlphaFoldDB; P57993; -.
DR SMR; P57993; -.
DR STRING; 272631.ML0304; -.
DR EnsemblBacteria; CAC29812; CAC29812; CAC29812.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 2.
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 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; SSF56112; 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