ID   PKNG_MYCBO              Reviewed;         750 AA.
AC   P65729; A0A1R3XXF1; P96256; X2BEZ4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Serine/threonine-protein kinase PknG;
DE            EC=2.7.11.1;
GN   Name=pknG; OrderedLocusNames=BQ2027_MB0418C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
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DR   EMBL; LT708304; SIT98994.1; -; Genomic_DNA.
DR   RefSeq; NP_854081.1; NC_002945.3.
DR   RefSeq; WP_003402100.1; NC_002945.4.
DR   AlphaFoldDB; P65729; -.
DR   SMR; P65729; -.
DR   TCDB; 9.B.321.1.1; the actinobacterial nutrient-sensing signal transduction pathway controlling glutamate metabolism (sigt) family.
DR   PATRIC; fig|233413.5.peg.456; -.
DR   Proteomes; UP000001419; 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   SUPFAM; SSF48452; TPR-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..750
FT                   /note="Serine/threonine-protein kinase PknG"
FT                   /id="PRO_0000171214"
FT   DOMAIN          151..396
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         157..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   750 AA;  81577 MW;  CFC6E54DBE19569F CRC64;
     MAKASETERS GPGTQPADAQ TATSATVRPL STQAVFRPDF GDEDNFPHPT LGPDTEPQDR
     MATTSRVRPP VRRLGGGLVE IPRAPDIDPL EALMTNPVVP ESKRFCWNCG RPVGRSDSET
     KGASEGWCPY CGSPYSFLPQ LNPGDIVAGQ YEVKGCIAHG GLGWIYLALD RNVNGRPVVL
     KGLVHSGDAE AQAMAMAERQ FLAEVVHPSI VQIFNFVEHT DRHGDPVGYI VMEYVGGQSL
     KRSKGQKLPV AEAIAYLLEI LPALSYLHSI GLVYNDLKPE NIMLTEEQLK LIDLGAVSRI
     NSFGYLYGTP GFQAPEIVRT GPTVATDIYT VGRTLAALTL DLPTRNGRYV DGLPEDDPVL
     KTYDSYGRLL RRAIDPDPRQ RFTTAEEMSA QLTGVLREVV AQDTGVPRPG LSTIFSPSRS
     TFGVDLLVAH TDVYLDGQVH AEKLTANEIV TALSVPLVDP TDVAASVLQA TVLSQPVQTL
     DSLRAARHGA LDADGVDFSE SVELPLMEVR ALLDLGDVAK ATRKLDDLAE RVGWRWRLVW
     YRAVAELLTG DYDSATKHFT EVLDTFPGEL APKLALAATA ELAGNTDEHK FYQTVWSTND
     GVISAAFGLA RARSAEGDRV GAVRTLDEVP PTSRHFTTAR LTSAVTLLSG RSTSEVTEEQ
     IRDAARRVEA LPPTEPRVLQ IRALVLGGAL DWLKDNKAST NHILGFPFTS HGLRLGVEAS
     LRSLARVAPT QRHRYTLVDM ANKVRPTSTF
//