PKNE_MYCTO
ID PKNE_MYCTO Reviewed; 566 AA.
AC P9WI76; L0TA94; O08149; P72001;
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 PknE;
DE EC=2.7.11.1;
GN Name=pknE; OrderedLocusNames=MT1785;
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: Important for survival of the bacterium in the host during
CC infection. Promotes the survival of infected macrophages by activating
CC multiple signaling responses and suppressing apoptosis of macrophages
CC during nitrate stress. May contribute to the adaptation of
CC M.tuberculosis during stress conditions by maintaining the cellular
CC integrity (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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC Dephosphorylated by PstP (By similarity). {ECO:0000250}.
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; AE000516; AAK46058.1; -; Genomic_DNA.
DR PIR; H70985; H70985.
DR RefSeq; WP_003898998.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI76; -.
DR SMR; P9WI76; -.
DR EnsemblBacteria; AAK46058; AAK46058; MT1785.
DR KEGG; mtc:MT1785; -.
DR PATRIC; fig|83331.31.peg.1915; -.
DR HOGENOM; CLU_000288_47_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Serine/threonine-protein kinase; Stress response;
KW Transferase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..566
FT /note="Serine/threonine-protein kinase PknE"
FT /id="PRO_0000428055"
FT TOPO_DOM 1..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 16..275
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 7
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 566 AA; 60512 MW; C31534068DE60FE4 CRC64;
MDGTAESREG TQFGPYRLRR LVGRGGMGDV YEAEDTVRER IVALKLMSET LSSDPVFRTR
MQREARTAGR LQEPHVVPIH DFGEIDGQLY VDMRLINGVD LAAMLRRQGP LAPPRAVAIV
RQIGSALDAA HAAGATHRDV KPENILVSAD DFAYLVDFGI ASATTDEKLT QLGNTVGTLY
YMAPERFSES HATYRADIYA LTCVLYECLT GSPPYQGDQL SVMGAHINQA IPRPSTVRPG
IPVAFDAVIA RGMAKNPEDR YVTCGDLSAA AHAALATADQ DRATDILRRS QVAKLPVPST
HPVSPGTRWP QPTPWAGGAP PWGPPSSPLP RSARQPWLWV GVAVAVVVAL AGGLGIALAH
PWRSSGPRTS APPPPPPADA VELRVLNDGV FVGSSVAPTT IDIFNEPICP PCGSFIRSYA
SDIDTAVADK QLAVRYHLLN FLDDQSHSKN YSTRAVAASY CVAGQNDPKL YASFYSALFG
SDFQPQENAA SDRTDAELAH LAQTVGAEPT AISCIKSGAD LGTAQTKATN ASETLAGFNA
SGTPFVWDGS MVVNYQDPSW LARLIG
