PKNJ_MYCTU
ID PKNJ_MYCTU Reviewed; 589 AA.
AC P9WI67; 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 42.
DE RecName: Full=Serine/threonine-protein kinase PknJ;
DE EC=2.7.11.1;
GN Name=pknJ; OrderedLocusNames=Rv2088; ORFNames=MTCY49.28;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
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=ATCC 25618 / H37Rv;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, PHOSPHORYLATION
RP AT THR-179, DEPHOSPHORYLATION, AND MUTAGENESIS OF LYS-43; HIS-78; THR-168;
RP SER-172 AND THR-179.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20520732; DOI=10.1371/journal.pone.0010772;
RA Arora G., Sajid A., Gupta M., Bhaduri A., Kumar P., Basu-Modak S.,
RA Singh Y.;
RT "Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical
RT characterization and identification of novel substrate pyruvate kinase A.";
RL PLoS ONE 5:E10772-E10772(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: In vitro, phosphorylates various substrates such as EmbR,
CC PepE, MmaA4, Pyk, LldD and GroEL2. {ECO:0000269|PubMed:20185505,
CC ECO:0000269|PubMed:20520732}.
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, ECO:0000269|PubMed:20520732};
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 ECO:0000269|PubMed:20520732};
CC -!- ACTIVITY REGULATION: Activated by certain divalent metal cations, such
CC as cobalt, manganese, nickel or magnesium. Zinc or iron ions do not
CC affect activity. {ECO:0000269|PubMed:20520732}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20185505,
CC ECO:0000269|PubMed:20520732}.
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, ECO:0000269|PubMed:20520732}.
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; AL123456; CCP44863.1; -; Genomic_DNA.
DR PIR; C70767; C70767.
DR RefSeq; NP_216604.1; NC_000962.3.
DR RefSeq; WP_003410735.1; NZ_NVQJ01000061.1.
DR AlphaFoldDB; P9WI67; -.
DR SMR; P9WI67; -.
DR STRING; 83332.Rv2088; -.
DR iPTMnet; P9WI67; -.
DR PaxDb; P9WI67; -.
DR DNASU; 888322; -.
DR GeneID; 888322; -.
DR KEGG; mtu:Rv2088; -.
DR TubercuList; Rv2088; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; LYYSGMT; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0050897; F:cobalt ion binding; IDA:MTBBASE.
DR GO; GO:0016151; F:nickel cation binding; IDA:MTBBASE.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:MTBBASE.
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; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="Serine/threonine-protein kinase PknJ"
FT /id="PRO_0000171222"
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:0000305|PubMed:20520732"
FT MUTAGEN 43
FT /note="K->A: Lack of kinase activity."
FT /evidence="ECO:0000269|PubMed:20520732"
FT MUTAGEN 78
FT /note="H->A: Lack of phosphorylation."
FT /evidence="ECO:0000269|PubMed:20520732"
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 ECO:0000269|PubMed:20520732"
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 172
FT /note="S->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:20520732"
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"
FT MUTAGEN 179
FT /note="T->A: Decreases phosphorylation."
FT /evidence="ECO:0000269|PubMed:20520732"
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
