ID V9XE69_9NOCA Unreviewed; 769 AA.
AC V9XE69;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-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=Y013_10155 {ECO:0000313|EMBL:AHD21013.1}, Y013_14275
GN {ECO:0000313|EMBL:AHD21741.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21741.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD21741.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD21741.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD21013.1; -; Genomic_DNA.
DR EMBL; CP006996; AHD21741.1; -; Genomic_DNA.
DR AlphaFoldDB; V9XE69; -.
DR KEGG; rpy:Y013_10155; -.
DR KEGG; rpy:Y013_14275; -.
DR PATRIC; fig|1435356.3.peg.2035; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR Proteomes; UP000018781; Chromosome.
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:AHD21741.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AHD21741.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 147..414
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84148 MW; 3AB6B56EE0F96957 CRC64;
MTAMSDEPEP ADTPSADSGP ATERGPGPVP ATRPESTQRS SIWSGSSSQR SSSQRSSNRR
IRPRGTQRRR IAGLVDVPVP TTKDPVDAVL RDPHVSEGKR FCAKCGQPVG RSTPSGPGPT
EGDCPQCGTH FQFTPALHRG DLVAGQYEVQ GCLAHGGLGW IYLAIDRNVS DRWVVLKGLL
QGGDAEAQAV AVAERQFLAE VSHPSIVQIY NFVEHPSPDG TPMGYIVMEY LGGHTLRTVL
DNYPPPNRIP VEQAIAYMLE VLPALQYLHD IGLVYNDLKP ENIMVTDEQI ELIDLGAVSA
IEGYGYLYGT PGYQAPEIVR TGPTVASDIY TVGRTLAVLT LDMPSDKGRY RDGLPTPEQA
PLLDEFDSFH RLLLRATNPD PQQRFSSADE LHGQLTGVLR EILSKKLGTE HPGLSRLFSP
PRTTFGTDEA LVPTDVYADG IERDPKLRGQ DVAAALPVPL LDPNDPSAAL LAAAVHSEPQ
QTLDSLRHAR ENGVGRVVGA SDVSFSKEIT LAEVRAHLDL GQVDSAVEIL TRLERESGDD
WRMDWYAGIA ELLQDDYEAA FTRFDKVLQA LPGEIAPKIA LGATAELTLQ HWESDDPDAW
RRFCEQSYRV VWRTDHAVVS AAFGLARQLT ARDEIRAAVD VLDEVPTTSR HHSAATMTAA
LILLRGDRVE EISEADLREA AHRIASLPPD EGRALQMRAL VLGTALEWVR SGRASSREYD
RILDVPFTEK GLRLGTEAAL RQLARNAPSR THRYTLVDLA NAIRPRSLT
//