ID   PKAB_STRCO              Reviewed;         417 AA.
AC   P54740; Q9L061; Q9L1S2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Serine/threonine-protein kinase PkaB;
DE            EC=2.7.11.1;
GN   Name=pkaB; OrderedLocusNames=SCO2973; ORFNames=SCE50.01, SCE59.32c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=7883195; DOI=10.1016/0378-1119(94)00789-u;
RA   Urabe H., Ogawara H.;
RT   "Cloning, sequencing and expression of serine/threonine kinase-encoding
RT   genes from Streptomyces coelicolor A3(2).";
RL   Gene 153:99-104(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- PTM: Autophosphorylated mainly at Thr.
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; D86821; BAA13169.1; -; Genomic_DNA.
DR   EMBL; AL939114; CAD55460.1; -; Genomic_DNA.
DR   PIR; JC4071; JC4071.
DR   RefSeq; NP_733588.1; NC_003888.3.
DR   RefSeq; WP_011028691.1; NZ_VNID01000010.1.
DR   AlphaFoldDB; P54740; -.
DR   SMR; P54740; -.
DR   STRING; 100226.SCO2973; -.
DR   GeneID; 1098406; -.
DR   KEGG; sco:SCO2973; -.
DR   PATRIC; fig|100226.15.peg.3031; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   InParanoid; P54740; -.
DR   OMA; THTSMRV; -.
DR   PhylomeDB; P54740; -.
DR   BRENDA; 2.7.11.1; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..417
FT                   /note="Serine/threonine-protein kinase PkaB"
FT                   /id="PRO_0000171233"
FT   DOMAIN          9..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          279..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   417 AA;  43417 MW;  3D66720FF17D3DE4 CRC64;
     MARKIGSRYT AHQILGRGSA GTVWLGEGPD GPVAIKLLRE DLASDQELVS RFVQERTALL
     GLDHPHVVSV RDLVVDGNDL ALVMDLVRGT DLRTRLDRER RLAPEAAVAV VADVADGLAA
     AHAAGVVHRD VKPENVLLDM QGPLGPGGSH PALLTDFGVA KLIDTPRRTR ATKIIGTPDY
     LAPEIVEGLP PRAAVDIYAL ATVLYELLAG FTPFGGGHPG AVLRRHVTET VVPLPGIPDE
     LWQLLVQCLA KAPASRLRAS ELSARLRELL PMLAGMAPLD VDEPDAEQPE DAPDASAASP
     AAPVSTAEPV RRRGAVPLVP GAKPADSNRD THTSMRVPAP DELAGGARGT ARAPRASGAP
     RPGSARNRAA TRRRRIAVGA GAVALVAAIG VGTWLATGGD EDGGGPQDTR NSAPAAP