ID A0A172UU35_9MYCO Unreviewed; 757 AA.
AC A0A172UU35;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A7U43_27060 {ECO:0000313|EMBL:ANE82430.1};
OS Mycobacterium adipatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE82430.1, ECO:0000313|Proteomes:UP000077143};
RN [1] {ECO:0000313|EMBL:ANE82430.1, ECO:0000313|Proteomes:UP000077143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE82430.1,
RC ECO:0000313|Proteomes:UP000077143};
RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT sp. YC-RL4.";
RL Submitted (MAY-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; CP015596; ANE82430.1; -; Genomic_DNA.
DR RefSeq; WP_068001340.1; NZ_CP015596.1.
DR AlphaFoldDB; A0A172UU35; -.
DR STRING; 1682113.A7U43_27060; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000077143; 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:ANE82430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077143};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:ANE82430.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..429
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 82191 MW; F9AA0014C567FA46 CRC64;
MNDDDPGTQP ASLAELDALA EPEDGEDSVA TMRPMATQAV YRPDFDDTDR ASTVSTEPSE
NITTWTRPRS PIRRLGGGLV EVPRVYERDP LTALMTNPVV AEAKRFCWNC NRPVGRASKK
DADGPARAGL SEGFCPRCGS PFSFLPQLSP GDTVADQYRI KGCIAHGGLG WVYLAFDTNV
NGRPVVLKGL VHSGDAEAQA TAMAERQFLA AVTHPAIVKI FNFVEHADKH GEPVGYIVME
YVGGTSLKQP KGVKLPVAQA IAYMLEILPA LGYLHSLGLV YNDLKPENIM VTAEQLKLID
LGAVSRINSF GYLYGTPGYQ APEIVRTGPT VQTDIYTVGR TLAALTLKLR TRKGRYVDGL
PEDDPVLAKY DSFGRLLRRA IDPDPNRRFA SADEMSSQLM GVLREVVAQD SGVPRPGLST
VFSPPRSTFG VDLLVAHTDV YLDGQVHSEK LTAPEIVKAL QVPLVDPADV GAPILSATVL
SQPVQTLDSL RAARHGTLDS EGIDLSESVE LPLMEARALL DLGDVAKATR KLDDLVERVG
WRWRIAWFRG VAALLTADYD TATKYFTEVL DTLPGELAPK LALAATAELA GSSDERRFYQ
TVWRTDNGII SAGFGLARAQ SAEGERDDAV RTLDQVPPTS RHFTVARLTS SVTLLSGRSI
NEVSEQQIRS AARRVEALPE SEPRVLQIRA LVLGTAMDWL ADNTASTNHI LGFPFTQHGL
QLGVEAALRG LARVAPTQEH RYALVDLANS VRPTSTF
//