PKAA_STRCO
ID PKAA_STRCO Reviewed; 543 AA.
AC P54739;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein kinase PkaA;
DE EC=2.7.11.1;
GN Name=pkaA; OrderedLocusNames=SCO2974; ORFNames=SCE50.02c;
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 and slightly at Ser.
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; BAA13168.1; -; Genomic_DNA.
DR EMBL; AL939114; CAB87324.1; -; Genomic_DNA.
DR PIR; JC4070; JC4070.
DR RefSeq; NP_627197.1; NC_003888.3.
DR RefSeq; WP_003975838.1; NZ_VNID01000010.1.
DR AlphaFoldDB; P54739; -.
DR SMR; P54739; -.
DR STRING; 100226.SCO2974; -.
DR GeneID; 1098407; -.
DR KEGG; sco:SCO2974; -.
DR PATRIC; fig|100226.15.peg.3032; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_63_44_11; -.
DR InParanoid; P54739; -.
DR OMA; WQNQLRA; -.
DR PhylomeDB; P54739; -.
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..543
FT /note="Serine/threonine-protein kinase PkaA"
FT /id="PRO_0000171232"
FT DOMAIN 8..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 303..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Pro residues"
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 14..22
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"
SQ SEQUENCE 543 AA; 58182 MW; 0E1965520FA0C200 CRC64;
MRPVGSKYLL EEPLGRGATG TVWRARQRET AGAEAAVAGQ PGETVAIKVL KEELASDADI
VMRFLRERSV LLRLTHPNIV RVRDLVVEGE LLALVMDLID GPDLHRYLRE NGPLTPVAAA
LLTAQIADAL AASHADGVVH RDLKPANVLL KQTGGEMHPM LTDFGIARLA DSPGLTRTHE
FVGTPAYVAP ESAEGRPQTS AVDVYGAGIL LYELVTGRPP FGGGSALEVL HQHLSAEPRR
PSTVPDPLWT VIERCLRKNP DDRPSAENLA RGLRVVAEGI GVHANSAQIG AAENVGALLA
PDPAPAQVPG APDAAYDPNG ATSVLPHTSG PAGAADPTAV LPSTGAPDPT AVMPPVPPGQ
PGAPGQGGPE DPHPWQNQLR AARDRNEQTQ VQYLDPNQDP LRRRPQRQVS RPPQQPRQAP
QGPPPQQPGY GYPQQQQPQR YATPQPQQPQ RYAPPPAPEP QQPRREPRPP RQRSANPMRI
PGLGCLKGCL VTVVVLFVAG WLVWELSPLQ EWIGTGKGYW DQLTDWFTTV TDWIGDLGGS
GGG
