PKNL_MYCTU
ID PKNL_MYCTU Reviewed; 399 AA.
AC P9WI63; L0TAE8; O53510;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Serine/threonine-protein kinase PknL;
DE EC=2.7.11.1;
GN Name=pknL; OrderedLocusNames=Rv2176; ORFNames=MTV021.09;
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 IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-48.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18276158; DOI=10.1016/j.pep.2007.12.012;
RA Lakshminarayan H., Narayanan S., Bach H., Sundaram K.G., Av-Gay Y.;
RT "Molecular cloning and biochemical characterization of a serine threonine
RT protein kinase, PknL, from Mycobacterium tuberculosis.";
RL Protein Expr. Purif. 58:309-317(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY,
RP PHOSPHORYLATION AT THR-32; THR-62; THR-173; THR-175 AND THR-323, AND
RP MUTAGENESIS OF LYS-48; SER-171; THR-173; SER-174 AND THR-175.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18175374; DOI=10.1002/pmic.200700442;
RA Canova M.J., Veyron-Churlet R., Zanella-Cleon I., Cohen-Gonsaud M.,
RA Cozzone A.J., Becchi M., Kremer L., Molle V.;
RT "The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates
RT Rv2175c: mass spectrometric profiling of the activation loop
RT phosphorylation sites and their role in the recruitment of Rv2175c.";
RL Proteomics 8:521-533(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19457863; DOI=10.1074/jbc.m109.019653;
RA Cohen-Gonsaud M., Barthe P., Canova M.J., Stagier-Simon C., Kremer L.,
RA Roumestand C., Molle V.;
RT "The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-
RT binding protein regulated by phosphorylation.";
RL J. Biol. Chem. 284:19290-19300(2009).
CC -!- FUNCTION: Phosphorylates the DNA-binding protein Rv2175c. May be
CC involved in the regulation of cell division and cell envelope
CC biosynthesis. {ECO:0000269|PubMed:18175374,
CC ECO:0000269|PubMed:19457863}.
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:18175374, ECO:0000269|PubMed:18276158,
CC ECO:0000269|PubMed:19457863};
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:18175374,
CC ECO:0000269|PubMed:18276158, ECO:0000269|PubMed:19457863};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18175374};
CC Single-pass membrane protein {ECO:0000305|PubMed:18175374}.
CC -!- PTM: Autophosphorylated. Thr-173 is required for autophosphorylation
CC and transphosphorylation activities. Thr-175 is not necessary for
CC autophosphorylation activity, but is required for full kinase activity.
CC {ECO:0000269|PubMed:18175374}.
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; CCP44953.1; -; Genomic_DNA.
DR PIR; B70936; B70936.
DR RefSeq; NP_216692.1; NC_000962.3.
DR RefSeq; WP_003899202.1; NZ_NVQJ01000083.1.
DR AlphaFoldDB; P9WI63; -.
DR SMR; P9WI63; -.
DR STRING; 83332.Rv2176; -.
DR iPTMnet; P9WI63; -.
DR PaxDb; P9WI63; -.
DR DNASU; 888340; -.
DR GeneID; 45426152; -.
DR GeneID; 888340; -.
DR KEGG; mtu:Rv2176; -.
DR PATRIC; fig|83332.111.peg.2422; -.
DR TubercuList; Rv2176; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; EFVWARQ; -.
DR PhylomeDB; P9WI63; -.
DR BRENDA; 2.7.11.1; 3445.
DR Proteomes; UP000001584; Chromosome.
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: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; IDA:MTBBASE.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..399
FT /note="Serine/threonine-protein kinase PknL"
FT /id="PRO_0000171226"
FT TOPO_DOM 1..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 19..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 312..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 32
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18175374"
FT MOD_RES 62
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18175374"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18175374"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18175374"
FT MOD_RES 323
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18175374"
FT MUTAGEN 48
FT /note="K->M: Lack of kinase activity."
FT /evidence="ECO:0000269|PubMed:18175374,
FT ECO:0000269|PubMed:18276158"
FT MUTAGEN 171
FT /note="S->A: Does not affect autophosphorylation and
FT transphosphorylation activities."
FT /evidence="ECO:0000269|PubMed:18175374"
FT MUTAGEN 173
FT /note="T->A: Strong decrease in autophosphorylation
FT activity. Lack of transphosphorylation activity."
FT /evidence="ECO:0000269|PubMed:18175374"
FT MUTAGEN 174
FT /note="S->A: Does not affect autophosphorylation and
FT transphosphorylation activities."
FT /evidence="ECO:0000269|PubMed:18175374"
FT MUTAGEN 175
FT /note="T->A: Decrease in autophosphorylation activity. Does
FT not affect transphosphorylation activity."
FT /evidence="ECO:0000269|PubMed:18175374"
SQ SEQUENCE 399 AA; 42834 MW; 1E63000018942C89 CRC64;
MVEAGTRDPL ESALLDSRYL VQAKIASGGT STVYRGLDVR LDRPVALKVM DSRYAGDEQF
LTRFRLEARA VARLNNRALV AVYDQGKDGR HPFLVMELIE GGTLRELLIE RGPMPPHAVV
AVLRPVLGGL AAAHRAGLVH RDVKPENILI SDDGDVKLAD FGLVRAVAAA SITSTGVILG
TAAYLSPEQV RDGNADPRSD VYSVGVLVYE LLTGHTPFTG DSALSIAYQR LDADVPRASA
VIDGVPPQFD ELVACATARN PADRYADAIA MGADLEAIAE ELALPEFRVP APRNSAQHRS
AALYRSRITQ QGQLGAKPVH HPTRQLTRQP GDCSEPASGS EPEHEPITGQ FAGIAIEEFI
WARQHARRMV LVWVSVVLAI TGLVASAAWT IGSNLSGLL
