ID A0A1G4WGQ0_9MYCO Unreviewed; 763 AA.
AC A0A1G4WGQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=SAMN02799620_03347 {ECO:0000313|EMBL:SCX22665.1};
OS Mycolicibacterium fluoranthenivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX22665.1, ECO:0000313|Proteomes:UP000199707};
RN [1] {ECO:0000313|Proteomes:UP000199707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
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DR EMBL; FMUB01000006; SCX22665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4WGQ0; -.
DR STRING; 1502745.SAMN02799620_03347; -.
DR Proteomes; UP000199707; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SCX22665.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 164..406
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 46..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 82975 MW; 4C2CC09CF3D9469F CRC64;
MADPDTGTEP EDPGTRPASL ADLEEFEDFD SDSVATVRPM ATQAVYRPDF GDSERFARSS
GGTATTEPTE HLTTATRPRS PTRRLGGGLV EIPRVTERNP LAALMTNPVV AESKRFCWNC
GKRVGRASAK DGTPARSEGT CPYCGSAYSF LPQLSPGDMV VDQYLIKGCI AHGGLGWVYL
AFDTNVNYRP VVLKGLVHSG DAEAQATAMA ERQFLAEVTH PAIVKIFNFV EHADKHGDPV
GYIVMEYVGG TSLKQGKGTR LPVAQAIAYM LEILPALGYL HSLGLVYNDL KPENIMVTEE
QLKLIDLGAV SRINSFGFLY GTPGYQAPEI VRTGPTVQTD IYTVGRTLAA LTLNLRTRKG
RYVDGLPDDD PVLTTYDSFG RLLRRAIDPD PRRRFTSAEE MSGQLLGVLR EVVAQDTRVP
RPGLSTVFSP PRSTFGVDLL VAHTDVYRDG QVHSAKLTAP EIVKALQVPL VDPADVGAPI
LSATVLSQPV QTLDSLRAAR HGTLDSEGID LSESVELPLM EVRALLDLGD VSKATRKLDD
LAERIGWRWR LVWFRGVAAL LTADFETATK YFTEVLDTLP GELAPKVALA ATAELAGTAD
ERRFYETVWR TDNGIISAGF GLARAQSADG DRDDAVRTLD LVPATSRHFT TARLTSAVTL
LSGRSINEVS ERQIRDAARR VEALPESEPR VLQIRALVLG TAMDWLADNT ASTNHILGFP
FTQHGLQLGV EASLRSLARV APTQAHRYAL VDLANSVRPM STF
//