PKNG_MYCTO
ID PKNG_MYCTO Reviewed; 750 AA.
AC P9WI72; L0T3M0; P65728; P96256;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Serine/threonine-protein kinase PknG;
DE EC=2.7.11.1;
GN Name=pknG; OrderedLocusNames=MT0423;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Phosphorylates GarA. May play a role in metabolic regulation
CC via control of the phosphorylation status of GarA. Plays a crucial role
CC in the survival of mycobacteria within host macrophages, by blocking
CC the intracellular degradation of mycobacteria in lysosomes. Required
CC for intrinsic antibiotic resistance (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- SUBUNIT: Homodimer. Interacts with the FHA domain of GarA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Also detected in growth media, suggesting that it
CC can be translocated into host macrophages under specific conditions.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44647.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK44647.1; ALT_INIT; Genomic_DNA.
DR PIR; H70628; H70628.
DR RefSeq; WP_003402100.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI72; -.
DR SMR; P9WI72; -.
DR EnsemblBacteria; AAK44647; AAK44647; MT0423.
DR KEGG; mtc:MT0423; -.
DR PATRIC; fig|83331.31.peg.452; -.
DR HOGENOM; CLU_011707_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; TPR repeat; Transferase; Virulence.
FT CHAIN 1..750
FT /note="Serine/threonine-protein kinase PknG"
FT /id="PRO_0000428057"
FT DOMAIN 151..396
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 536..569
FT /note="TPR"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 157..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 750 AA; 81577 MW; CFC6E54DBE19569F CRC64;
MAKASETERS GPGTQPADAQ TATSATVRPL STQAVFRPDF GDEDNFPHPT LGPDTEPQDR
MATTSRVRPP VRRLGGGLVE IPRAPDIDPL EALMTNPVVP ESKRFCWNCG RPVGRSDSET
KGASEGWCPY CGSPYSFLPQ LNPGDIVAGQ YEVKGCIAHG GLGWIYLALD RNVNGRPVVL
KGLVHSGDAE AQAMAMAERQ FLAEVVHPSI VQIFNFVEHT DRHGDPVGYI VMEYVGGQSL
KRSKGQKLPV AEAIAYLLEI LPALSYLHSI GLVYNDLKPE NIMLTEEQLK LIDLGAVSRI
NSFGYLYGTP GFQAPEIVRT GPTVATDIYT VGRTLAALTL DLPTRNGRYV DGLPEDDPVL
KTYDSYGRLL RRAIDPDPRQ RFTTAEEMSA QLTGVLREVV AQDTGVPRPG LSTIFSPSRS
TFGVDLLVAH TDVYLDGQVH AEKLTANEIV TALSVPLVDP TDVAASVLQA TVLSQPVQTL
DSLRAARHGA LDADGVDFSE SVELPLMEVR ALLDLGDVAK ATRKLDDLAE RVGWRWRLVW
YRAVAELLTG DYDSATKHFT EVLDTFPGEL APKLALAATA ELAGNTDEHK FYQTVWSTND
GVISAAFGLA RARSAEGDRV GAVRTLDEVP PTSRHFTTAR LTSAVTLLSG RSTSEVTEEQ
IRDAARRVEA LPPTEPRVLQ IRALVLGGAL DWLKDNKAST NHILGFPFTS HGLRLGVEAS
LRSLARVAPT QRHRYTLVDM ANKVRPTSTF
