PKNI_MYCTU
ID PKNI_MYCTU Reviewed; 585 AA.
AC P9WI69; 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 42.
DE RecName: Full=Serine/threonine-protein kinase PknI;
DE EC=2.7.11.1;
GN Name=pknI; OrderedLocusNames=Rv2914c; ORFNames=MTCY338.02c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, AND AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15177288; DOI=10.1016/j.pep.2004.03.011;
RA Gopalaswamy R., Narayanan P.R., Narayanan S.;
RT "Cloning, overexpression, and characterization of a serine/threonine
RT protein kinase pknI from Mycobacterium tuberculosis H37Rv.";
RL Protein Expr. Purif. 36:82-89(2004).
RN [3]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16256441; DOI=10.1016/j.tube.2005.04.002;
RA Singh A., Singh Y., Pine R., Shi L., Chandra R., Drlica K.;
RT "Protein kinase I of Mycobacterium tuberculosis: cellular localization and
RT expression during infection of macrophage-like cells.";
RL Tuberculosis 86:28-33(2006).
RN [4]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19341393; DOI=10.1111/j.1574-6968.2009.01570.x;
RA Gopalaswamy R., Narayanan S., Chen B., Jacobs W.R., Av-Gay Y.;
RT "The serine/threonine protein kinase PknI controls the growth of
RT Mycobacterium tuberculosis upon infection.";
RL FEMS Microbiol. Lett. 295:23-29(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Plays an important role in slowing down the growth of
CC mycobacteria within the infected host. {ECO:0000269|PubMed:19341393}.
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:15177288, ECO:0000269|PubMed:16256441};
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:15177288,
CC ECO:0000269|PubMed:16256441};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15177288};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16256441}. Cell
CC membrane {ECO:0000269|PubMed:16256441}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16256441}. Note=More abundant in the cytosol than
CC in the cell membrane.
CC -!- INDUCTION: Expression decreases during infection of human macrophages.
CC {ECO:0000269|PubMed:16256441}.
CC -!- PTM: Autophosphorylated at serine and threonine residues.
CC -!- DISRUPTION PHENOTYPE: Mutants show increased growth within macrophages
CC and a hypervirulence phenotype in severe combined immunodeficiency
CC mice. {ECO:0000269|PubMed:19341393}.
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; AL123456; CCP45716.1; -; Genomic_DNA.
DR PIR; B70747; B70747.
DR RefSeq; NP_217430.1; NC_000962.3.
DR RefSeq; WP_003900593.1; NZ_NVQJ01000006.1.
DR PDB; 5M06; X-ray; 2.00 A; A/B=1-256.
DR PDB; 5M07; X-ray; 2.50 A; A/B=1-256.
DR PDB; 5M08; X-ray; 3.03 A; A/B=1-256.
DR PDB; 5M09; X-ray; 2.98 A; A/B=1-256.
DR PDB; 5XKA; X-ray; 1.60 A; A/B=1-280.
DR PDB; 5XLL; X-ray; 2.20 A; A/B=402-585.
DR PDB; 5XLM; X-ray; 2.20 A; A/B=372-585.
DR PDBsum; 5M06; -.
DR PDBsum; 5M07; -.
DR PDBsum; 5M08; -.
DR PDBsum; 5M09; -.
DR PDBsum; 5XKA; -.
DR PDBsum; 5XLL; -.
DR PDBsum; 5XLM; -.
DR AlphaFoldDB; P9WI69; -.
DR SMR; P9WI69; -.
DR STRING; 83332.Rv2914c; -.
DR PaxDb; P9WI69; -.
DR GeneID; 45426901; -.
DR GeneID; 887642; -.
DR KEGG; mtu:Rv2914c; -.
DR TubercuList; Rv2914c; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; EGYYIAM; -.
DR BRENDA; 2.7.11.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MTBBASE.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0040009; P:regulation of growth rate; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000171220"
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"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 111..130
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:5XKA"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:5XKA"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:5XLM"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:5XLM"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:5XLL"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 502..511
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:5XLM"
FT STRAND 536..545
FT /evidence="ECO:0007829|PDB:5XLM"
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
