ID F8E1K8_CORRG Unreviewed; 833 AA.
AC F8E1K8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AEI08513.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AEI08513.1};
GN Name=pknG {ECO:0000313|EMBL:AEI08513.1};
GN OrderedLocusNames=CRES_0150 {ECO:0000313|EMBL:AEI08513.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI08513.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI08513.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
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; CP002857; AEI08513.1; -; Genomic_DNA.
DR AlphaFoldDB; F8E1K8; -.
DR STRING; 662755.CRES_0150; -.
DR KEGG; crd:CRES_0150; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000000492; 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; 1.
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:AEI08513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000492};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AEI08513.1}; Transferase {ECO:0000313|EMBL:AEI08513.1}.
FT DOMAIN 184..465
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 91678 MW; 444A1A8CACD0070E CRC64;
MPFDPFADDD EEDIADANSG THVDTNEDTI DETEVHTEAV AFDPFADDED TTDGTEVHTE
AVPFDPFADD DEEDTDSVES FASNDPDEIT GPLTKRAGKD GASNKKKPVS NLEPGERSRR
EALSEFRRLR GTRRRGAQVA GGMVRLPFIP PTDPEKAVID PTSAIEKGVE PPTLKSGDII
AGQYEILGPI AHGGLGWVYI AIDHNVADRY VVLKGMMATE NEHEKAVAES ERAFLADITH
PGIVKIFNFI DDPRVEGGFI VMEYVGGPSL RDRRRRMPRN LLEVDVAIGY ILEVLPALDY
LHSRGVVYND LKPDNIIITE DQVKLIDLGA VTGIGAFGHI FGTKGFQAPE IATTGPTVAS
DIYTVGRTLA SLIVPLKVEN GAYTSQLPTP DEEPLFREYM SLYRLLLRAT NPDPQVRFGS
ASAMVNQLVG VLREILAIRD GRQFAHLDTR FTAQRSTYGT KHIVFRTDQL LDGVERSVEI
SPSEVVAALP TPLTDTSDPG AALLSAASFT ETSDLMDTLD SAMKNPDMEN SVEIPLTMVR
AHLDVGQTAE AKALLGSLEP RMGNDWRFHW HSGVVGLLSG EYATAQKCFN KVLYILPGEP
APKLALAATD ELLLQQQGVN TSKLLDAEAT RAASALAYAQ RIPVDDYTGV PGWDHVTLDP
VALRFHAMRL YGLVWATNPT TVSSAFGLAR QLMAEGLVDS AVNALDRVPQ NSRHNRLARF
TTILILISDA SLLTEARIRR AARRLATMPT NEPRLEQIRL AVMSAALNWL RRRLDEGSGP
VSTEPILDAE FTERGLRLGL ERGLRHMARQ TQFPLHRFRL VDMANKIRPR TWF
//
