PKNG_MYCBO
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 03-AUG-2022, entry version 107.
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; Actinobacteria; Corynebacteriales; 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 OMA; PHCGSAY; -.
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: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; SSF48452; SSF48452; 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 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
