PKNG_MYCS2
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 03-AUG-2022, entry version 98.
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; Actinobacteria; Corynebacteriales; 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.MSMEI_0770; -.
DR PRIDE; A0QQK3; -.
DR EnsemblBacteria; ABK71095; ABK71095; MSMEG_0786.
DR EnsemblBacteria; AFP37250; AFP37250; 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 OMA; PHCGSAY; -.
DR OrthoDB; 1377603at2; -.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 2.
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 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; SSF56112; 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
