ID   A1T2Z1_MYCVP            Unreviewed;       755 AA.
AC   A1T2Z1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Mvan_0703 {ECO:0000313|EMBL:ABM11541.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11541.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM11541.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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; CP000511; ABM11541.1; -; Genomic_DNA.
DR   RefSeq; WP_011777978.1; NZ_JACKSD010000046.1.
DR   AlphaFoldDB; A1T2Z1; -.
DR   STRING; 350058.Mvan_0703; -.
DR   KEGG; mva:Mvan_0703; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   Proteomes; UP000009159; 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   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABM11541.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:ABM11541.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          153..427
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  82060 MW;  2D267EE8E9AED2EE CRC64;
     MTEPEDLDGG QGTQPAGYSD LADDTMSTMR PMATQAVFRP NFFDDEEDSD ALHSGDTEPQ
     LTTTTVTRHM SPTRRLGGGL VEIPRVPARD PLAALMTDPV VAESKRFCWN CGRPVGRSTK
     DGRALSEGWC PHCGSAYSFL PQLNVGDIVA DQYEIKGCIA HGGLGWVYLA FDKNVNDRPV
     VLKGLVHSGD AEAQAIAMAE RQFLAQVTHP GIVKIYNFVE HEDKHGNPVG YIVMEYVGGT
     SLKQATAQKG TRLPVAEAIG FMLEILPALG HLHSIGLVYN DLKPENVMVT EDQLKLIDLG
     AVSRINSFGY LYGTPGYQAP EIVRTGPTVA TDMYTVGRTL AALTLKLRTR KGRYVDGLPE
     DDPVLATYDS YGRLLRRAID PDPRRRFQSA EEMSSQLMGV LREVVAKDTG VPRPGLSTVF
     SRSRSTFGVD LLVAHTDVYL DGQVHSEKLT AQEIVRALQV PLVDPTDVGA TILSAIVLSQ
     PVQTLDSLRA ARHGTLDSEG IDLSESVELP LMEVRALLDL GDVAKATRKL DDLAERVGWR
     WRLVWFRAVS ELLTADYDSA TKHFNEVLDT LPGELAPKLA LAATAELAGS ADERSFYNTV
     WSTDNGVISA GFGLARAQSA AGDRDAAVRT LDEVPATSRH FTTARLTSAV TLLSGRSSSE
     ITEQHIRDAA RRVEALPDSE PRVLQIRALV LGTAMDWLAD NTASTNHILG FPFTEHGLAL
     GVEASLRSLA RVAPTQAHRY ALVDLANSVR PMSTF
//