ID A0A1X1RCT0_MYCFA Unreviewed; 766 AA.
AC A0A1X1RCT0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:BBY98857.1};
GN ORFNames=AWC04_10945 {ECO:0000313|EMBL:ORV03142.1}, MFAL_23240
GN {ECO:0000313|EMBL:BBY98857.1};
OS Mycolicibacterium fallax (Mycobacterium fallax).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1793 {ECO:0000313|EMBL:ORV03142.1, ECO:0000313|Proteomes:UP000193484};
RN [1] {ECO:0000313|EMBL:ORV03142.1, ECO:0000313|Proteomes:UP000193484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44179 {ECO:0000313|EMBL:ORV03142.1,
RC ECO:0000313|Proteomes:UP000193484};
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:BBY98857.1, ECO:0000313|Proteomes:UP000467101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 6405 {ECO:0000313|EMBL:BBY98857.1,
RC ECO:0000313|Proteomes:UP000467101};
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:BBY98857.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6405 {ECO:0000313|EMBL:BBY98857.1};
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; AP022603; BBY98857.1; -; Genomic_DNA.
DR EMBL; LQOJ01000039; ORV03142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1RCT0; -.
DR STRING; 1793.AWC04_10945; -.
DR KEGG; mfx:MFAL_23240; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000193484; Unassembled WGS sequence.
DR Proteomes; UP000467101; 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; 1.
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:ORV03142.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193484};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:ORV03142.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 167..438
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 82652 MW; 962660283C270B31 CRC64;
MRDDEIDTCD EGPGTQRADP FADDDQPDSG PGTQRADVLV DTAAGGRPMA TQAVYRPNFA
DDDEDDDAFS VDSEQATSAP TRAVAPIRQV GGGLVEIPAI PELDPLAALM VDPVVMEAKR
FCWNCGKPVG RGRGNTPGPV AGTCPHCGSE YSFLPQLGPG DMVADQYEIK GCIAHGGLGW
IYLAVDHNVN ERPVVLKGLV HSGDAEAQAI AMAERRFLAE VAHPSIVKIY NFVEHPDSRG
EPVGFIVMEY VGGRSLKQRG EQRLSVPQAI AYMLEILPAL GYLHSIGLCY NDLKPDNIML
TGDQLKLIDL GAVSRINSFG FLYGTPGYQA PEIVRTGPTV LSDLYTVGRT LAALTLRLPA
KKGRYLDGLP ADDPVLARYD SFARLLLRAT DPDPRRRFGS AEEMSAQLLG VLREVVAQDT
GIPRPGLSTV FSPSRSTFGV ELLVAHTDVY LDGKPHSEKL TAAEIITALP VPLVDPTDVG
AKVLSATLLS QPVQALDSLR AARHGRLDTE GVNLRDSVEL PLMEIRALLD LGDVSKATRK
LDELSGRVGR AWRLVWFRAV SELLTADYES ATRHFTEVLN TLPGELAPKL ALGATAELSG
SAGEERHYRT VWQTDNGVIA AGFGLARAQS VAGERDAAVR TLDEVPATSR HFATARLTSA
MTLLSGRSIS EVTEEQIREA ARRVDALPES EPRVPQIRAL VLGTALDWIA DNTADPHHIL
GFPFTESGLQ LGVEASLRAL ARLAPSQQHR YALVDMANTV RPMTTF
//