PKNB_MYCBO
ID PKNB_MYCBO Reviewed; 626 AA.
AC P0A5S5; A0A1R3XU24; P71584; X2BDS6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Serine/threonine-protein kinase PknB;
DE EC=2.7.11.1;
GN Name=pknB; OrderedLocusNames=BQ2027_MB0014C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC 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: 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; LT708304; SIT98359.1; -; Genomic_DNA.
DR RefSeq; NP_853684.1; NC_002945.3.
DR RefSeq; WP_003400356.1; NC_002945.4.
DR AlphaFoldDB; P0A5S5; -.
DR SMR; P0A5S5; -.
DR EnsemblBacteria; SIT98359; SIT98359; BQ2027_MB0014C.
DR GeneID; 45423973; -.
DR PATRIC; fig|233413.5.peg.18; -.
DR OMA; DPDYRYQ; -.
DR Proteomes; UP000001419; 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; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..626
FT /note="Serine/threonine-protein kinase PknB"
FT /id="PRO_0000171206"
FT TOPO_DOM 1..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 356..422
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 423..490
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 491..557
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 558..626
FT /note="PASTA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 299..323
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 169
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 294
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 295
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 309
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 66510 MW; 6C27EEBE9D5A453B CRC64;
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL RDIVHTEGPM TPKRAIEVIA
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSGNSV TQTAAVIGTA
QYLSPEQARG DSVDARSDVY SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH
EGLSADLDAV VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI NTFGGITRDV
QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI GTDPAANTSV SAGDEITVNV
STGPEQREIP DVSTLTYAEA VKKLTAAGFG RFKQANSPST PELVGKVIGT NPPANQTSAI
TNVVIIIVGS GPATKDIPDV AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP
AGTTVPVDSV IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH
NRVVYQNPPA GTGVNRDGII TLRFGQ
