ID A0A132T875_9MYCO Unreviewed; 760 AA.
AC A0A132T875;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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=ASJ79_21735 {ECO:0000313|EMBL:KWX67393.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX67393.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX67393.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX67393.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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:KWX67393.1}.
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DR EMBL; LMVQ01000116; KWX67393.1; -; Genomic_DNA.
DR RefSeq; WP_067954785.1; NZ_LMVQ01000116.1.
DR AlphaFoldDB; A0A132T875; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000070146; 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:KWX67393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070146};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:KWX67393.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 155..432
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 83034 MW; 3AC77F4C6E830895 CRC64;
MADPEDFDED PGTQPASFAD LADDTMSTMR PMATQAVYRP NFFDDDDDDS DGRFHTGDTE
PQLNTTTVTR HMSPTRRLGG GLVEIPRVRA RDPLAALMTD PVVAESKRFC WNCGRPVGRS
TKDGKGPSEG WCPHCGSAYS FLPQLNVGDI VADQYEIKGC IAHGGLGWVY LAFDKNVNDR
PVVLKGLVHS GDAEAQAIAM AERQFLAEVT HPGIVKIYNF VEHDDKHGNP VGYIVMEYVG
GTSLKQAAPH RKSERSLLPV AEAIGFMLEI LPALGYLHSL GLVYNDLKPE NIMVTEDQLK
LIDLGAVSRI NSFGYLYGTP GYQAPEIVRT GPTVATDIYT VGRTLASLTL KLRTRKGRYV
DGLPEDDPVL REYDSFGRLL RRAIDPDPRR RFQSAEEMSS QLMGVLREVV AKDTGVPRPG
LSTTFSPSRS TFGIDLLVAH TDVYLDGQVH SEKLTAQEIV RALQVPLVDP TDVGATVLSA
TVLSEPVQTL DSLRAARHGA LDSEGVDLSQ SVELPLMEAR ALLDLGDVAK ATRKLDDLAE
RVGWRWRLVW FRAVSELLTA DYDSATKHFT EVLDMLPGEL APKLALAATA ELAGSADERK
FYDTVWSTDH GVISAGFGLA RAQSAAGDRD AAVRTLDEVP ATSRYFTTAR LTSAVTLLSG
RSSSEITEQH IRDAARRVEA LPDTEPRVLQ IRALVLGTAM DWLADNTAST NHILGFPFTE
HGLQLGVEAS LRSLARVAPT QAHRYALVDL ANSVRPMSTF
//
