ID A0A1R0U963_9MYCO Unreviewed; 768 AA.
AC A0A1R0U963;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A5736_20910 {ECO:0000313|EMBL:OMC14701.1};
OS Mycobacterium sp. SP-6446.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834162 {ECO:0000313|EMBL:OMC14701.1, ECO:0000313|Proteomes:UP000187139};
RN [1] {ECO:0000313|Proteomes:UP000187139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-6446 {ECO:0000313|Proteomes:UP000187139};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OMC14701.1}.
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DR EMBL; MBEM01000140; OMC14701.1; -; Genomic_DNA.
DR RefSeq; WP_076246674.1; NZ_MBEM01000140.1.
DR AlphaFoldDB; A0A1R0U963; -.
DR Proteomes; UP000187139; 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; 2.
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 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:OMC14701.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:OMC14701.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 165..440
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 83785 MW; 8A33601AD1A214FE CRC64;
MAEPMKKADK NREAPEPADQ PDEDVSPATQ PPDTQTGGMP TGRLQATQAL FRPDFDDDDD
DFPLIHGVDT EPQERTVATR VLPPTRQLGG GLVEIPRVRD IDPLEALMTN PVVPESKRFC
WNCGKPVGRS GEEGKGASEG WCPSCGSPYT FLPQLNPGDI VAGQYEVKGC IAHGGLGWVY
LAVDHNVNDR PVVLKGLVHS GDAEAQAIAM AERQFLAEVV HPQIVQIFNF VEHTDRHGDP
VGYIVMEYIG GQSLKRGLKD GKADKLPVAE AVAYLLEILP ALSYLHSIGL VYNDLKPENI
MLTEEQLKLI DLGAVSRINS FGYLYGTPGF QAPEIVRTGP TVATDIYTVG RTLAALTLNL
RTRNGRYVDG LPEDDPVLTT YDSFGRLLRR ATDPDPRRRF STADEMSAQL MGVLREVVAQ
DTGVPRPGLS TIFSPSRSTF GVDLLVAHTD VYLDGQVHSE RLTAREIVTA LPVPLVDPTD
VAAPVLQATV LSQPVQTLDS LRAARHGSLD AEGADVSESV ELPLMEVRAL LDLGDVAKAT
RKIDDLAERV GWRWRLVWYR AVAELLTGDY DSAIKHFTEV LDTFPGELAP KLALAATAEL
AGSTDEHMYY ETVWKTNDGV ISAAFGLARA LSAEGDRAAA VRTLDEVPAT SRHFTTARLT
SAVTLMSGRS TNEITEEQIR DAARRVEALP PTEPRVLQIR ALVLGGAMDW LEDNDASTNH
ILGFPFTEHG LRLGVEASLR ALARVAPTQR HRYTLVDMAN KVRPTSTF
//