ID A0A024JTR1_9MYCO Unreviewed; 755 AA.
AC A0A024JTR1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BN973_01067 {ECO:0000313|EMBL:CDO86722.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO86722.1};
RN [1] {ECO:0000313|EMBL:CDO86722.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86722.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO86722.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86722.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) 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};
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DR EMBL; HG964446; CDO86722.1; -; Genomic_DNA.
DR RefSeq; WP_036466398.1; NZ_LQPY01000021.1.
DR AlphaFoldDB; A0A024JTR1; -.
DR STRING; 47839.BN973_01067; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
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:CDO86722.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CDO86722.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 155..427
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 82291 MW; CB52CDC03CFAC3B5 CRC64;
MTEAEHDADA EDTDPGTQPP DAQTGATTGR AHATQALFRP EWDDDDDDLP HLTLGGVDTE
PQDRMTVATR VLPPTRQLGG GLVEIPRIRD IDPLEALMTN PVVPEHKRFC WNCGKPVGRS
TSEGKGESEG KCPSCGSPYS FLPQLNPGDI VANQYEVKGC IAHGGLGWVY LAVDHNVNDR
PVVLKGLVHS GDAEAQAIAM AERQFLAEVV HPQIVQIFNF VEHTDRHGDP VGYIVMEYIG
GQSLKRGKKD PRLPVAEAIA YLLEILPALS YLHSIGLVYN DLKPENIMLT EEQLKLIDLG
AVSRVNSFGY LYGTPGYQAP EIVRTGPTIA TDIYTVGRTL AALTLNLRTR NGRYVDGLPE
DDPVLSTYDS FGRLLRRAID PDPRRRFGSA EEISAQLTGV LREVVAQDSG VPRPGLSTLF
SPSRSTFGVD LSVAHTDVYL DGQVHSEKLT AREIVTALSV PLVDPTDVAS PVLQATVLSQ
PVQTLDSLRA ARHGSLAAEG IDVSESVELP LMEVRALLDL GDVAKATRKL DDLAERVGWR
WRLVWFRAVA ELLTGDYDSA IKHFTEVLDT FPGELAPKLA LAATGELAGH VDVDKFYKTV
WRTNDGVISA AFGLARSLSA EGDRIGAVRT LDEVPATSRH FTTARLTSAV TLLSGRSTSE
ITEEQIRDAA RRVEALPPTE PRVLQIRALV LGGAMDWLET NTASTNHILG FPFTQHGLRL
GVEASLRSLA RVAPTQRHRY TLVDMANRVR PTSTF
//