PKNA_MYCLE
ID PKNA_MYCLE Reviewed; 437 AA.
AC P54743; Q50184;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine/threonine-protein kinase PknA;
DE EC=2.7.11.1;
GN Name=pknA; OrderedLocusNames=ML0017;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8969512; DOI=10.1099/13500872-142-11-3147;
RA Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G.,
RA Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
RT "Gene arrangement and organization in an approximately 76 kb fragment
RT encompassing the oriC region of the chromosome of Mycobacterium leprae.";
RL Microbiology 142:3147-3161(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Protein kinase that regulates many aspects of mycobacterial
CC physiology. Is a key component of a signal transduction pathway that
CC regulates cell growth, cell shape and cell division via phosphorylation
CC of target proteins. {ECO:0000250|UniProtKB:P9WI83}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {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; Z70722; CAA94719.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29525.1; -; Genomic_DNA.
DR PIR; A86911; A86911.
DR PIR; T10010; T10010.
DR RefSeq; NP_301143.1; NC_002677.1.
DR RefSeq; WP_010907468.1; NC_002677.1.
DR AlphaFoldDB; P54743; -.
DR SMR; P54743; -.
DR STRING; 272631.ML0017; -.
DR EnsemblBacteria; CAC29525; CAC29525; CAC29525.
DR KEGG; mle:ML0017; -.
DR PATRIC; fig|272631.5.peg.21; -.
DR Leproma; ML0017; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_63_44_11; -.
DR OMA; AYCEYRV; -.
DR Proteomes; UP000000806; 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 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 3: Inferred from homology;
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..437
FT /note="Serine/threonine-protein kinase PknA"
FT /id="PRO_0000171204"
FT TOPO_DOM 1..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 13..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 277..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 281..355
FT /note="PRPNQTPSSGRASPTTIPSSTQARAAVACGTKTPAPRRSRPSTSGNRPPPAR
FT NTFSSGQRALLWAAGMLGALAII -> RGPTKHHLPAGPLQRPSRQAHRPEQLLLAAPR
FT LRHLADPDRQQAEIARRRRETRSRLDNARCSGPPGCSERWRSS (in Ref. 1;
FT CAA94719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 46312 MW; F08F07240C7C29D0 CRC64;
MSPRIGVMLS GRYRLHRLIA TGGMGQVWEA VDSRLGRRVA VKVLKGEFSS DPEFIERFRA
EARTTAMLNH PGIASVHDYG ESHMDGEGRT AYLVMELVNG EPLNSVLKRT GRLSLRHALD
MLEQTGRALQ IAHAAGLVHR DVKPGNILIT PTGQVKITDF GIAKAVDAAP VTQTGMVMGT
AQYIAPEQAL GHDATPASDV YSLGVIGYEV VSGKRPFTGD GALTVAMKHI KEPPPPLPAD
LPPNVRELIE ITLVKNPGMR YPSGGLFAEA VAAVRAGHRP PRPNQTPSSG RASPTTIPSS
TQARAAVACG TKTPAPRRSR PSTSGNRPPP ARNTFSSGQR ALLWAAGMLG ALAIIIAVLI
VINSYAGNEQ HQPPTPTVTD TGTPPATKTL SGFPAAYCEY RVNWTNHKEI SNSGLPKQAA
RAQLAGATDI SPVAGQT
