ID   Q4JXQ3_CORJK            Unreviewed;       863 AA.
AC   Q4JXQ3;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Serine/threonine protein kinase PknG {ECO:0000313|EMBL:CAI36404.1};
DE            EC=2.7.1.37 {ECO:0000313|EMBL:CAI36404.1};
GN   Name=pknG {ECO:0000313|EMBL:CAI36404.1};
GN   OrderedLocusNames=jk0252 {ECO:0000313|EMBL:CAI36404.1};
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36404.1, ECO:0000313|Proteomes:UP000000545};
RN   [1] {ECO:0000313|EMBL:CAI36404.1, ECO:0000313|Proteomes:UP000000545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411 {ECO:0000313|EMBL:CAI36404.1,
RC   ECO:0000313|Proteomes:UP000000545};
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
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DR   EMBL; CR931997; CAI36404.1; -; Genomic_DNA.
DR   RefSeq; WP_011272973.1; NC_007164.1.
DR   AlphaFoldDB; Q4JXQ3; -.
DR   STRING; 306537.jk0252; -.
DR   GeneID; 3432410; -.
DR   KEGG; cjk:jk0252; -.
DR   PATRIC; fig|306537.10.peg.262; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16918; PknG_TPR; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CAI36404.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:CAI36404.1}; Transferase {ECO:0000313|EMBL:CAI36404.1}.
FT   DOMAIN          133..378
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  93076 MW;  B35F231C527E90F4 CRC64;
     MQSNNNSEPE ERTEAVEFDP FADSEPEERT EAVPFDPFAD DEDTDATEQH TDPVGTPANA
     MDSGERSRIE ALSTFRKRRG TYRSGASVAD GMVQLPFIAP TNPEDAVIDP SAAIEKGVEA
     PTLKSGDIIA GQYEILGPIA HGGLGWVYIA IDHNVADRYV VLKGMMATEN EQERAVAESE
     RAFLADITHP GIVKIFNFID DPRSPGGFIV MEYVGGPSLR GQRRKLAAGV LDLDVAIGYI
     LEILPALDYL HSRGVVYNDL KPDNILITED QVKLIDLGAV TGIGAFGHIF GTKGFQAPEI
     AKTGPTVASD IYTVGRTLAA LIVKLPVEDG VYAPGLPTPD EEPLFREYLS LYRLLLRATD
     EDPEARFSSA TAMANQLIGV LREILAIRDG RHYPHLYTRF TAQRSTFGTK HIVFRTDQLV
     DGVVRSVEIS VPEVVSALPT PLADSQDPGY GLLSATSFTE AGDLLDTLRA AYAQPELKHS
     VEIPLTMVRA LLDVGQTREA HDLLDELKPW LEKDWRFQWH SGVAALLTGQ FAEAQKFFNR
     VLYILPGEPA PKLALAATDE LLLQQQGVNS TKLLSEHVSR AASALAYAQK LPVKDYTGVP
     GWEHVTLDPV SLRFHAMRLY GLVWATNQST VSSAFGLARQ LRAEGMVDSA VAALDRLPQA
     SRHNRLARLT SILLLISDAN SLTESRIRRA ARRLETLPTN EPRLPQVRIA VLSAGLNWLR
     GASDGSDGAA GIAGGGAGNT GTGGAGAAGA GAGAGRGRGS AGGTGAGGGA EAGSSRGSRK
     SKGKRKLGAV TRINRGSPTR ANEASQLKRQ AAAAPLFDVQ FTERGLRTGL EKSLRQLARQ
     APFARHRYDL VDMANQIRPR TWF
//