PKNK_MYCTO
ID PKNK_MYCTO Reviewed; 1110 AA.
AC P9WI64; L0TEA2; P95078;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Serine/threonine-protein kinase PknK;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase K;
GN Name=pknK; OrderedLocusNames=MT3165;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Key microbial factor involved in regulation of early and late
CC events in tuberculosis infection, and in host-pathogen interactions.
CC {ECO:0000250}.
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 -!- SUBUNIT: Forms oligomeric complexes in solution. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Secreted, cell wall. Note=Probably attached to the cell
CC membrane through interactions mediated by its C-terminal region. May be
CC secreted during infection (By similarity). {ECO:0000250}.
CC -!- PTM: Can autophosphorylate the carboxyl terminal region in addition to
CC Thr-179 and Thr-181. {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; AE000516; AAK47501.1; -; Genomic_DNA.
DR PIR; A70652; A70652.
DR RefSeq; WP_003899905.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI64; -.
DR SMR; P9WI64; -.
DR EnsemblBacteria; AAK47501; AAK47501; MT3165.
DR KEGG; mtc:MT3165; -.
DR PATRIC; fig|83331.31.peg.3411; -.
DR HOGENOM; CLU_006325_2_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cell wall; Cytoplasm; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Secreted;
KW Serine/threonine-protein kinase; Transferase; Virulence.
FT CHAIN 1..1110
FT /note="Serine/threonine-protein kinase PknK"
FT /id="PRO_0000428061"
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 149
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"
FT MOD_RES 179
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1110 AA; 119418 MW; 2F81BF18BCD3E472 CRC64;
MTDVDPHATR RDLVPNIPAE LLEAGFDNVE EIGRGGFGVV YRCVQPSLDR AVAVKVLSTD
LDRDNLERFL REQRAMGRLS GHPHIVTVLQ VGVLAGGRPF IVMPYHAKNS LETLIRRHGP
LDWRETLSIG VKLAGALEAA HRVGTLHRDV KPGNILLTDY GEPQLTDFGI ARIAGGFETA
TGVIAGSPAF TAPEVLEGAS PTPASDVYSL GATLFCALTG 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
