ID A0A1A1WL82_9MYCO Unreviewed; 756 AA.
AC A0A1A1WL82;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A5730_12525 {ECO:0000313|EMBL:OBF07156.1};
OS Mycobacterium sp. ACS4054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834119 {ECO:0000313|EMBL:OBF07156.1, ECO:0000313|Proteomes:UP000091876};
RN [1] {ECO:0000313|EMBL:OBF07156.1, ECO:0000313|Proteomes:UP000091876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS4054 {ECO:0000313|EMBL:OBF07156.1,
RC ECO:0000313|Proteomes:UP000091876};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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};
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:OBF07156.1}.
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DR EMBL; LZHV01000044; OBF07156.1; -; Genomic_DNA.
DR RefSeq; WP_067900095.1; NZ_LZHV01000044.1.
DR AlphaFoldDB; A0A1A1WL82; -.
DR STRING; 1834119.A5730_12525; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000091876; 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:OBF07156.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:OBF07156.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 157..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 82587 MW; E26A1E4796222B5B CRC64;
MAEPEKTEQP ESAEDVNPGT QPPDTQGGPV TGRIQATQAL FRPDFDDDDD DDFPHISLGT
MDSDPQLTVG TRVLPPVRHL GGGLVEIPRV RDIDPVEALM TNPVVPEGKR FCWNCGKPVG
RSGKEGKGKS EGWCPACGSA YSFLPQLNPG DIVAGQYEVK GCIAHGGLGW VYLAVDHNVN
DRPVVLKGLV HSGDAEAQAI AMAERQFLAE VVHPQIVQIF NFVEHKDRQG NPVGYIVMEY
IGGQPLKHGK DKKLPVAEAI AYLLEILPAL TYLHSIGLVY NDLKPENIML TEEQLKLIDL
GAVSRVNSFG YLYGTPGFQA PEIVRTGPTV ATDIYTVGRT LAALTVNLPT RNGRYVDGLP
EDDPVLTEYD SYRRLLRRAT DPDPRRRFAS TEELSAQLMG VLREVVAQDT GVPRPGLSTI
FSPSRSTFGV DLLVAHTDVY LDGQVHSERL TAREIVTALQ VPLVDPADVA APVLQATVLS
QPVQTLDSLR AARHGTLDAD GVEVSESIEL PLMEVRALLD LGDVAKATRK LDDLAERVGW
QWRLVWYRAV AELLTGDYDS ATTHFTEVLD TFPGELAPKL ALAATAELAG DVDEQKYYQT
VWKTNDGVIS AAFGLARWLS TAGDRAAAVR TLDEVPPTSR HFTTARLTSA VTLLSGRSKS
EISEEDIRDA ARRVEALPPT EPRVLQIRAL VLGCAMDWLE DNEASTNHIL GFPFTEHGLR
LGVEAALRNL ARVAPTQRHR YALVDMANKV RPTSTF
//
