(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 119.
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}.
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; NC_003888.3.
DR   SMR; P54739; -.
DR   STRING; 100226.SCO2974; -.
DR   PRIDE; P54739; -.
DR   EnsemblBacteria; CAB87324; CAB87324; CAB87324.
DR   GeneID; 1098407; -.
DR   KEGG; sco:SCO2974; -.
DR   PATRIC; fig|100226.15.peg.3032; -.
DR   eggNOG; ENOG4108UGD; Bacteria.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000115552; -.
DR   InParanoid; P54739; -.
DR   KO; K08884; -.
DR   OMA; WQNQLRA; -.
DR   PhylomeDB; P54739; -.
DR   BRENDA; 2.7.11.1; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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;
DR   PRODOM; P54739.
DR   SWISS-2DPAGE; P54739.
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   NP_BIND         14..22
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        301..481
FT                   /note="Gln/Pro-rich"
FT   ACT_SITE        142
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         48
FT                   /note="ATP"
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
//

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