ID A0A1X0JYM8_9MYCO Unreviewed; 754 AA.
AC A0A1X0JYM8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BST47_05015 {ECO:0000313|EMBL:ORB68018.1};
OS Mycolicibacterium tusciae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=75922 {ECO:0000313|EMBL:ORB68018.1, ECO:0000313|Proteomes:UP000192411};
RN [1] {ECO:0000313|EMBL:ORB68018.1, ECO:0000313|Proteomes:UP000192411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44153 {ECO:0000313|Proteomes:UP000192411};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORB68018.1}.
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DR EMBL; MVIM01000002; ORB68018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0JYM8; -.
DR STRING; 75922.BST47_05015; -.
DR eggNOG; COG0515; Bacteria.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000192411; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031634; PknG_rubred.
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; PF16919; PknG_rubred; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ORB68018.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:ORB68018.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 151..393
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 81920 MW; C910C68F246448B7 CRC64;
MAAVQSDESD PGTQPASLDD LEFDSAATLR PMATQAVFRP HFDDDSEGSS VGTGETEPQE
HTTATRALSP MRRLGGGLVE IPRVRAKDPL EALMTNPVVA EGKRFCWNCG RPVGRSSDDG
EALSEGWCPH CGSAYSFLPQ LSPGDMINDQ YEIKGCIAHG GLGWVYLAFD HNVNERPVVL
KGLVHSGDAE AQKIAMLERQ FLAEVTHPGI VKIYNFVEHD DKHGNPVGYI VMEYVGGTSL
KQARGEKVPV AQAIGYMLEI LPALGYLHSI GLTYNDLKPE NIMITEEQLK LIDLGAVSTI
NSFGYLYGTP GYQAPEIVRT GPTVATDIYT VGRTLAALTL NMRTRKGRYV DGLPEDDPVL
TEYDSFARLL RRAIDPDPRR RFASAEEMTS QLLGVLREVV ARDTGVPRPG LSTVFSASRS
TFGVDLLVAH TDVYLDGQVH SERLTAQDIV KALQVPLVDP ADVGATVLSA SVLTQPVQTL
DSLRAARHGA LDSEGIDLSE SVELPLMEVR ALLDLGDVAK ATRKLEDLAE RVGWRWRLVW
FRAVSAMLTA DYDSATKYFT EVLDTLPGEL APKLALAATA ELAGAQVDEA PQRKFYDTVW
STDNGVISAG FGLARSQSAA GDRDAAVRTL DQVPVMSRHF TTARLTSAVT LLSGRSTNEI
TEQHIRDAAR RVEALPDTEP RVLQIRALVL GTAMDWLADN TASTNHILGF PFTEHGLQLG
VEASLRALAR VAPTQGHRYA LVDLANSVRP TSTF
//