ID   PKNG_MYCS2              Reviewed;         760 AA.
AC   A0QQK3;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Serine/threonine-protein kinase PknG;
DE            EC=2.7.11.1;
GN   Name=pknG; OrderedLocusNames=MSMEG_0786, MSMEI_0770;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   INTERACTION WITH GARA.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA   O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA   Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT   "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL   Mol. Microbiol. 70:1408-1423(2008).
RN   [5]
RP   CATALYTIC ACTIVITY, AND LACK OF TRANSLATION IN VIVO.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=19210624; DOI=10.1111/j.1365-2958.2009.06612.x;
RA   Houben E.N., Walburger A., Ferrari G., Nguyen L., Thompson C.J., Miess C.,
RA   Vogel G., Mueller B., Pieters J.;
RT   "Differential expression of a virulence factor in pathogenic and non-
RT   pathogenic mycobacteria.";
RL   Mol. Microbiol. 72:41-52(2009).
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:0000269|PubMed:19210624};
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:0000269|PubMed:19210624};
CC   -!- SUBUNIT: Interacts with GarA in vitro. {ECO:0000269|PubMed:19019160}.
CC   -!- MISCELLANEOUS: When artificially expressed from expression vectors,
CC       encodes an active kinase, which is able to block the lysosomal delivery
CC       of mycobacteria inside macrophages. However, while PknG transcripts are
CC       found in M.smegmatis, expression of PknG is blocked on a translational
CC       level in this non-pathogenic species. This lack of efficient
CC       translation is caused by regulatory elements in the upstream region of
CC       the gene (PubMed:19210624). {ECO:0000305|PubMed:19210624}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CP000480; ABK71095.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37250.1; -; Genomic_DNA.
DR   RefSeq; WP_011727190.1; NZ_SIJM01000036.1.
DR   RefSeq; YP_885191.1; NC_008596.1.
DR   AlphaFoldDB; A0QQK3; -.
DR   SMR; A0QQK3; -.
DR   IntAct; A0QQK3; 1.
DR   STRING; 246196.MSMEG_0786; -.
DR   PaxDb; 246196-MSMEI_0770; -.
DR   GeneID; 66738961; -.
DR   KEGG; msg:MSMEI_0770; -.
DR   KEGG; msm:MSMEG_0786; -.
DR   PATRIC; fig|246196.19.peg.781; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..760
FT                   /note="Serine/threonine-protein kinase PknG"
FT                   /id="PRO_0000419491"
FT   DOMAIN          161..403
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         167..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   760 AA;  82645 MW;  417893787A19511B CRC64;
     MTSPENPDLP DADDAYVDSG PGTQPASLED LDMDSASTMR PMATQAVYRP EFDDTDGTSR
     GTVVTEAYDQ VTMATRALSP MRRLGGGLVE IPRVPERDPL TALMTNPVVA ESKRFCWNCG
     KPVGRSTPDG RALSEGWCPH CGSPYSFLPQ LSPGDIVADQ YEIKGCIAHG GLGWVYLAFD
     KNVNDRPVVL KGLVHSGDAE AQAIAMAERQ FLAEVTHPGI VKIYNFVEHE DKHGNPVGYI
     VMEYVGGTSL KQARGAKLPV AEAIGYMLEI LPALGYLHSI GLAYNDLKPE NIMITEEQLK
     LIDLGAVSRL NSYGYLYGTP GYQAPEIVRT GPTVATDIYT VGRTLAALTL SLRTRRGRYV
     DGLPSDDPVL ETYDSYHRLL RRAIDPDPRR RFTSAEEMSS QLLGVLREVV ATDTGVPRPG
     LSTVFSPSRS TFGVDLLVAH TDVYVDGQVH SEKLTAQEIV RALPVPLVDR TDVGAPMLVA
     SVLSEPVHTL DQLRAARHGA LDTEGIDLNE SVELPLMEVR ALLDLGDVAK ATRKLEDLAA
     RVGWRWRLVW FKAVSEMLSA DYDSATKHFT EVLDTLPGEL APKLALAATA ELAGTADELK
     FYKTVWSTDN GVISAGFGLA RAQSVAGERD MAVQTLDEVP PTSRHFTTAR LTSAVTLLSG
     RSTSEITEQH IRDAARRVEA LPDSEPRVLQ IRALVLGTAL DWLADNTASS NHILGFPFTE
     HGLKLGVEAS LRALARIAPT QSHRYALVDL ANSVRPMSTF
//