ID   PKNJ_MYCTO              Reviewed;         589 AA.
AC   P9WI66; L0T8S8; P65732; Q10697;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Serine/threonine-protein kinase PknJ;
DE            EC=2.7.11.1;
GN   Name=pknJ; OrderedLocusNames=MT2149;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
RP   PHOSPHORYLATION AT THR-168; THR-171 AND THR-173, MUTAGENESIS OF THR-168;
RP   THR-171 AND THR-173, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=20185505; DOI=10.1099/mic.0.038133-0;
RA   Jang J., Stella A., Boudou F., Levillain F., Darthuy E., Vaubourgeix J.,
RA   Wang C., Bardou F., Puzo G., Gilleron M., Burlet-Schiltz O., Monsarrat B.,
RA   Brodin P., Gicquel B., Neyrolles O.;
RT   "Functional characterization of the Mycobacterium tuberculosis
RT   serine/threonine kinase PknJ.";
RL   Microbiology 156:1619-1631(2010).
CC   -!- FUNCTION: In vitro, phosphorylates various substrates such as EmbR,
CC       PepE, MmaA4, LldD and GroEL2. {ECO:0000269|PubMed:20185505}.
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         Evidence={ECO:0000269|PubMed:20185505};
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; Evidence={ECO:0000269|PubMed:20185505};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20185505}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20185505};
CC       Single-pass membrane protein {ECO:0000269|PubMed:20185505}.
CC   -!- PTM: Autophosphorylated. Dephosphorylated by PstP.
CC       {ECO:0000269|PubMed:20185505}.
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; AAK46430.1; -; Genomic_DNA.
DR   PIR; C70767; C70767.
DR   RefSeq; WP_003410735.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI66; -.
DR   SMR; P9WI66; -.
DR   iPTMnet; P9WI66; -.
DR   EnsemblBacteria; AAK46430; AAK46430; MT2149.
DR   KEGG; mtc:MT2149; -.
DR   PATRIC; fig|83331.31.peg.2318; -.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; 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: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; 3.40.1000.70; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR026954; PknH-like_Extracell.
DR   InterPro; IPR038232; PknH-like_Extracell_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF14032; PknH_C; 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   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..589
FT                   /note="Serine/threonine-protein kinase PknJ"
FT                   /id="PRO_0000428060"
FT   TOPO_DOM        1..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..589
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          365..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         168
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:20185505"
FT   MOD_RES         171
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:20185505"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:20185505"
FT   MOD_RES         179
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         168
FT                   /note="T->A: Does not affect phosphorylation. Lack of
FT                   phosphorylation; when associated with A-171 and A-173."
FT                   /evidence="ECO:0000269|PubMed:20185505"
FT   MUTAGEN         171
FT                   /note="T->A: Lack of phosphorylation; when associated with
FT                   A-168 and A-173."
FT                   /evidence="ECO:0000269|PubMed:20185505"
FT   MUTAGEN         173
FT                   /note="T->A: Lack of phosphorylation; when associated with
FT                   A-168 and A-171."
FT                   /evidence="ECO:0000269|PubMed:20185505"
SQ   SEQUENCE   589 AA;  61595 MW;  E1E179150E2D348E CRC64;
     MAHELSAGSV FAGYRIERML GAGGMGTVYL ARNPDLPRSE ALKVLAAELS RDLDFRARFV
     READVAAGLD HPNIVAVHQR GQFEGRLWIA MQFVDGGNAE DALRAATMTT ARAVYVIGEV
     AKALDYAHQQ GVIHRDIKPA NFLLSRAAGG DERVLLSDFG IARALGDTGL TSTGSVLATL
     AYAAPEVLAG QGFDGRADLY SLGCALFRLL TGEAPFAAGA GAAVAVVAGH LHQPPPTVSD
     RVPGLSAAMD AVIATAMAKD PMRRFTSAGE FAHAAAAALY GGATDGWVPP SPAPHVISQG
     AVPGSPWWQH PVGSVTALAT PPGHGWPPGL PPLPRRPRRY RRGVAAVAAV MVVAAAAVTA
     VTMTSHQPRT ATPPSAAALS PTSSSTTPPQ PPIVTRSRLP GLLPPLDDVK NFVGIQNLVA
     HEPMLQPQTP NGSINPAECW PAVGGGVPSA YDLGTVIGFY GLTIDEPPTG TAPNQVGQLI
     VAFRDAATAQ RHLADLASIW RRCGGRTVTL FRSEWRRPVE LSTSVPEVVD GITTMVLTAQ
     GPVLRVREDH AIAAKNNVLV DVDIMTPDTS RGQQAVIGIT NYILAKIPG