PKNB_MYCLE
ID PKNB_MYCLE Reviewed; 622 AA.
AC P54744;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine/threonine-protein kinase PknB;
DE EC=2.7.11.1;
GN Name=pknB; OrderedLocusNames=ML0016;
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:P9WI81}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity).
CC {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; CAA94718.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29524.1; -; Genomic_DNA.
DR PIR; H86910; H86910.
DR PIR; T10009; T10009.
DR RefSeq; NP_301142.1; NC_002677.1.
DR RefSeq; WP_010907467.1; NC_002677.1.
DR AlphaFoldDB; P54744; -.
DR SMR; P54744; -.
DR STRING; 272631.ML0016; -.
DR EnsemblBacteria; CAC29524; CAC29524; CAC29524.
DR KEGG; mle:ML0016; -.
DR PATRIC; fig|272631.5.peg.20; -.
DR Leproma; ML0016; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_11; -.
DR OMA; DPDYRYQ; -.
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:0046872; F:metal ion 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 GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..622
FT /note="Serine/threonine-protein kinase PknB"
FT /id="PRO_0000171207"
FT TOPO_DOM 1..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 11..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 352..418
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 419..486
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 487..553
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 554..622
FT /note="PASTA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 381..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 93..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 140..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 166
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 172
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 303..304
FT /note="FG -> LC (in Ref. 1; CAA94718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 66187 MW; 9611B0FD93F2BA7C CRC64;
MTTPPHLSDR YELGDILGFG GMSEVHLARD IRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPS IVAVYDTGEA ETSAGPLPYI VMEYVDGATL RDIVHTDGPM PPQQAIEIVA
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSTSVT QTAAVIGTAQ
YLSPEQARGD SVDARSDVYS LGCVLYEILT GEPPFIGDSP VSVAYQHVRE DPIPPSQRHE
GISVDLDAVV LKALAKNPEN RYQTAAEMRA DLIRVHSGQP PEAPKVLTDA DRSCLLSSGA
GNFGVPRTDA LSRQSLDETE SDGSIGRWVA VVAVLAVLTI AIVAAFNTFG GNTRDVQVPD
VRGQVSADAI SALQNRGFKT RTLQKPDSTI PPDHVISTEP GANASVGAGD EITINVSTGP
EQREVPDVSS LNYTDAVKKL TSSGFKSFKQ ANSPSTPELL GKVIGTNPSA NQTSAITNVI
TIIVGSGPET KQIPDVTGQI VEIAQKNLNV YGFTKFSQAS VDSPRPTGEV IGTNPPKDAT
VPVDSVIELQ VSKGNQFVMP DLSGMFWADA EPRLRALGWT GVLDKGPDVD AGGSQHNRVA
YQNPPAGAGV NRDGIITLKF GQ
