PKNJ_MYCBO
ID PKNJ_MYCBO Reviewed; 589 AA.
AC P65733; A0A1R3Y092; Q10697; X2BK37;
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 PknJ;
DE EC=2.7.11.1;
GN Name=pknJ; OrderedLocusNames=BQ2027_MB2115;
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {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; SIU00722.1; -; Genomic_DNA.
DR RefSeq; NP_855764.1; NC_002945.3.
DR RefSeq; WP_003410735.1; NC_002945.4.
DR AlphaFoldDB; P65733; -.
DR SMR; P65733; -.
DR EnsemblBacteria; SIU00722; SIU00722; BQ2027_MB2115.
DR PATRIC; fig|233413.5.peg.2325; -.
DR OMA; LYYSGMT; -.
DR Proteomes; UP000001419; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..589
FT /note="Serine/threonine-protein kinase PknJ"
FT /id="PRO_0000171221"
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"
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
