ID   PKNI_MYCBO              Reviewed;         585 AA.
AC   P65731; A0A1R3Y2J8; Q10964; X2BMF5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Serine/threonine-protein kinase PknI {ECO:0000250|UniProtKB:P9WI69};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P9WI69};
GN   Name=pknI; OrderedLocusNames=BQ2027_MB2938C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Plays an important role in slowing down the growth of
CC       mycobacteria within the infected host. {ECO:0000250|UniProtKB:P9WI69}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:0000250|UniProtKB:P9WI69};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P9WI69};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P9WI69};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WI69}. Cell
CC       membrane {ECO:0000250|UniProtKB:P9WI69}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Autophosphorylated at serine and threonine residues.
CC       {ECO:0000250|UniProtKB:P9WI69}.
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; LT708304; SIU01559.1; -; Genomic_DNA.
DR   RefSeq; WP_003900593.1; NC_002945.4.
DR   AlphaFoldDB; P65731; -.
DR   SMR; P65731; -.
DR   GeneID; 45426901; -.
DR   KEGG; mbo:BQ2027_MB2938C; -.
DR   PATRIC; fig|233413.5.peg.3224; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   FunFam; 3.30.200.20:FF:000035; Serine/threonine protein kinase Stk1; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR063098; PknI_sensor.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF31220; PknI_sensor; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..585
FT                   /note="Serine/threonine-protein kinase PknI"
FT                   /id="PRO_0000171219"
FT   TOPO_DOM        1..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI69"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..585
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI69"
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        554..585
FT                   /note="Low complexity"
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="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI69"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         90
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI69"
FT   BINDING         92
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI69"
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
//