PKNI_MYCTO
ID PKNI_MYCTO Reviewed; 585 AA.
AC P9WI68; L0TB90; P65730; Q10964;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Serine/threonine-protein kinase PknI;
DE EC=2.7.11.1;
GN Name=pknI; OrderedLocusNames=MT2982;
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: Plays an important role in slowing down the growth of
CC mycobacteria within the infected host. {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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated at serine and threonine residues.
CC {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=AAK47308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK47308.1; ALT_INIT; Genomic_DNA.
DR PIR; B70747; B70747.
DR RefSeq; WP_003900593.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI68; -.
DR SMR; P9WI68; -.
DR EnsemblBacteria; AAK47308; AAK47308; MT2982.
DR GeneID; 45426901; -.
DR KEGG; mtc:MT2982; -.
DR PATRIC; fig|83331.31.peg.3222; -.
DR HOGENOM; CLU_000288_63_44_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..585
FT /note="Serine/threonine-protein kinase PknI"
FT /id="PRO_0000428059"
FT TOPO_DOM 1..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 12..252
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 546..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 585 AA; 61805 MW; E52EACFF4A69C3EC CRC64;
MALASGVTFA GYTVVRMLGC SAMGEVYLVQ HPGFPGWQAL KVLSPAMAAD DEFRRRFQRE
TEVAARLFHP HILEVHDRGE FDGQLWIAMD YVDGIDATQH MADRFPAVLP VGEVLAIVTA
VAGALDYAHQ RGLLHRDVNP ANVVLTSQSA GDQRILLADF GIASQPSYPA PELSAGADVD
GRADQYALAL TAIHLFAGAP PVDRSHTGPL QPPKLSAFRP DLARLDGVLS RALATAPADR
FGSCREFADA MNEQAGVAIA DQSSGGVDAS EVTAAAGEEA YVVDYPAYGW PEAVDCKEPS
ARAPAPAAPT PQRRGSMLQS AAGVLARRLD NFSTATKAPA SPTRRRPRRI LVGAVAVLLL
AGLFAVGIVI GRKTNTTATE VARPPTSGSA VPSAPTTTVA VTAPVPLDGT YRIEIQRSKQ
TYDYTPTPQP PDVNTWWAFR TSCTPTECLA AATMLDDNDH TQAKTPPVRP FLMQFGEGQW
KSRPETVQFP CVGPNGSPST QATTQLLALR PQPQGDLVGE MVVTVHSNEC GQQGAVIRIP
AVASRSGDLP PAVTVPDPAT IPDTPDTTST ATLTPPTTTA PGPGR
