ID   PKNK_MYCBO              Reviewed;        1110 AA.
AC   Q7TXA9; A0A1R3Y316; X2BNB1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Serine/threonine-protein kinase PknK;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase K;
GN   Name=pknK; OrderedLocusNames=BQ2027_MB3107C;
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT708304; SIU01732.1; -; Genomic_DNA.
DR   RefSeq; NP_856752.1; NC_002945.3.
DR   RefSeq; WP_003416064.1; NC_002945.4.
DR   AlphaFoldDB; Q7TXA9; -.
DR   SMR; Q7TXA9; -.
DR   PATRIC; fig|233413.5.peg.3414; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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   GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016236; Ser/Thr_kinase_PknK_prd.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000574; Ser/Thr_PK_PknK_prd; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1110
FT                   /note="Serine/threonine-protein kinase PknK"
FT                   /id="PRO_0000171223"
FT   DOMAIN          26..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          308..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         32..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1110 AA;  119446 MW;  3C2AD79972BCCDA0 CRC64;
     MTDVDPHATR RDLVPNIPAE LLEAGFDNVE EIGRGGFGVV YRCVQPSLDR AVAVKVLSTD
     LDRDNLERFL REQRAMGRLS GHPHIVTVLQ VGVLAGGRPF IVMPYHAKNS LETLIRRHGP
     LDWRETLSIG VKLAGALEAA HRVGTLHRDV KPGNILLTDY GEPQLTDFGI ARIAGGFETA
     TGVIAGSPAF TAPEVLEGAS PTPASDVYSL GATLFCVLTG HAAYERRSGE RVIAQFLRIT
     SQPIPDLRKQ GLPADVAAAI ERAMARHPAD RPATAADVGE ELRDVQRRNG VSVDEMPLPV
     ELGVERRRSP EAHAAHRHTG GGTPTVPTPP TPATKYRPSV PTGSLVTRSR LTDILRAGGR
     RRLILIHAPS GFGKSTLAAQ WREELSRDGA AVAWLTIDND DNNEVWFLSH LLESIRRVRP
     TLAESLGHVL EEHGDDAGRY VLTSLIDEIH ENDDRIAVVI DDWHRVSDSR TQAALGFLLD
     NGCHHLQLIV TSWSRAGLPV GRLRIGDELA EIDSAALRFD TDEAAALLND AGGLRLPRAD
     VQALTTSTDG WAAALRLAAL SLRGGGDATQ LLRGLSGASD VIHEFLSENV LDTLEPELRE
     FLLVASVTER TCGGLASALA GITNGRAMLE EAEHRGLFLQ RTEDDPNWFR FHQMFADFLH
     RRLERGGSHR VAELHRRASA WFAENGYLHE AVDHALAAGD PARAVDLVEQ DETNLPEQSK
     MTTLLAIVQK LPTSMVVSRA RLQLAIAWAN ILLQRPAPAT GALNRFETAL GRAELPEATQ
     ADLRAEADVL RAVAEVFADR VERVDDLLAE AMSRPDTLPP RVPGTAGNTA ALAAICRFEF
     AEVYPLLDWA APYQEMMGPF GTVYAQCLRG MAARNRLDIV AALQNFRTAF EVGTAVGAHS
     HAARLAGSLL AELLYETGDL AGAGRLMDES YLLGSEGGAV DYLAARYVIG ARVKAAQGDH
     EGAADRLSTG GDTAVQLGLP RLAARINNER IRLGIALPAA VAADLLAPRT IPRDNGIATM
     TAELDEDSAV RLLSAGDSAD RDQACQRAGA LAAAIDGTRR PLAALQAQIL HIETLAATGR
     ESDARNELAP VATKCAELGL SRLLVDAGLA
//