ID A0A1X1YN97_9MYCO Unreviewed; 761 AA.
AC A0A1X1YN97;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknG {ECO:0000313|EMBL:BBX98471.1};
GN ORFNames=AWC15_15150 {ECO:0000313|EMBL:ORW12589.1}, MLAC_37650
GN {ECO:0000313|EMBL:BBX98471.1};
OS Mycobacterium lacus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=169765 {ECO:0000313|EMBL:BBX98471.1, ECO:0000313|Proteomes:UP000466396};
RN [1] {ECO:0000313|EMBL:ORW12589.1, ECO:0000313|Proteomes:UP000193202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44577 {ECO:0000313|EMBL:ORW12589.1,
RC ECO:0000313|Proteomes:UP000193202};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBX98471.1, ECO:0000313|Proteomes:UP000466396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98471.1,
RC ECO:0000313|Proteomes:UP000466396};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBX98471.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98471.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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; AP022581; BBX98471.1; -; Genomic_DNA.
DR EMBL; LQPF01000025; ORW12589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1YN97; -.
DR STRING; 169765.AWC15_15150; -.
DR KEGG; mlj:MLAC_37650; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000193202; Unassembled WGS sequence.
DR Proteomes; UP000466396; 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:BBX98471.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000466396};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:ORW12589.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 161..404
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82738 MW; 141472D2CC36B763 CRC64;
MGKPTNKGLG SGSQDSDQED LGPSTQPADV LFTESSKIRP PSTQALFRPD FDEDDDFPHT
GGMDTEPQDR PTAATRVLPP VRQLGGGLVA IPRVPDIDPV KALMTNPVVP ESKRFCWNCG
RPVGRSGSEG KGASEGWCPY CGSPYSFLPQ LSPGDIVAGQ YEVKGCIAHG GLGWVYLAVD
HNVNDRPVVL KGLVHSGDAE AQAIAMAERQ FLAEVVHPAI VQIFNFVEHT DRHGDPVGYI
VMEYVGGQSL KRGRKQEKLP VAEAIAYLLE ILPALGYLHS IGLVYNDLKP ENIMLTEEQL
KLIDLGAVSR INSFGYLYGT PGFQAPEIVR TGPTVATDIY TVGRTLAALT LNLRTRNGRY
VDGLPEDDPV LAKYDSFGRL LRRAIDPDPR RRFASAEEMS GQLMGVLREA VAQDTGVPRP
GLSTIFSRTR STFGVNLLVA HTDVYLDGQV HSEKLTAKEI VTALQVPLVD PADVAAPVLQ
ATVLSEPVQT LDSLRAARHG ALAAEGIDLS ESIELPLMEV RALLDLGDVA KATRKLDDLA
ERVGWRWRLI WYRAVAELLT GDYDSASKHF TEVLDTFPGE VAPKMALAAT AELAGDAEAH
KFYQAVWRTD DGVISAAFGL ARSQSAEGDR MGAVRTLDEV PATSRHFTTA RLTSAVTLLS
GRSTSEITEE QIRDAARRVE ALPPTEPRVL QIRALVLGGA MDWLKDNQAS TNHILGFPFT
MHGLRLGVEA SLRSLARVAP TQRHRYTLVD MANKVRPTST F
//
