ID   SPKC_SYNY3              Reviewed;         535 AA.
AC   P74745;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Serine/threonine-protein kinase C;
DE            EC=2.7.11.1;
GN   Name=spkC; OrderedLocusNames=slr0599;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=12168951; DOI=10.1093/dnares/9.3.71;
RA   Kamei A., Yuasa T., Geng X., Ikeuchi M.;
RT   "Biochemical examination of the potential eukaryotic-type protein kinase
RT   genes in the complete genome of the unicellular Cyanobacterium
RT   synechocystis sp. PCC 6803.";
RL   DNA Res. 9:71-78(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AB046599; BAB17035.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18865.1; -; Genomic_DNA.
DR   PIR; S76953; S76953.
DR   AlphaFoldDB; P74745; -.
DR   SMR; P74745; -.
DR   IntAct; P74745; 5.
DR   STRING; 1148.1653955; -.
DR   PaxDb; P74745; -.
DR   EnsemblBacteria; BAA18865; BAA18865; BAA18865.
DR   KEGG; syn:slr0599; -.
DR   eggNOG; COG0515; Bacteria.
DR   InParanoid; P74745; -.
DR   OMA; TATFFEC; -.
DR   PhylomeDB; P74745; -.
DR   Proteomes; UP000001425; Chromosome.
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; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..535
FT                   /note="Serine/threonine-protein kinase C"
FT                   /id="PRO_0000171241"
FT   DOMAIN          12..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          371..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..423
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..528
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         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   535 AA;  58142 MW;  533CD9FC0E3D23D8 CRC64;
     MVTPLKLLNN RYRIIETLGR GGFGETFLAQ DTHMPSARKC VIKHLKPVLE NPEIPSWLRE
     RFHREAATLE ELGENHPQIP QLYAYFSEGE DFYLVQEWIP GLTLTQAHAQ KGNFSSTAVE
     ELLLGILPVL EFIHQRRIIH RDIKPDNIIL READGKPILI DFGIIKETMG TLVNPDGRSA
     YSVALGTPGY MASEQAAGRP VFSSDLYSLG LTAIFLLTGK TPQYLTSDSR TGEILWRQGA
     PQVSPTLAKV IDQAVRYHPR ERFNSATAMA QTLQGNFSNV PMTKGDRPGN TVANGKTKSN
     HQPTAPTLVV GTPYNANDTQ ATKVYTQEFT GYTETQEGSP LMKWVVMPLV VLLVIGGGMA
     AGFWVTSQRR NNPPPAVEEP TEETPIPLPS LEPRPNLFET PSPIPTPATP SPEPTPSPSP
     SPETTSSPTE DTITPMEPEP SLDEPAPIPE PKPSPSPTIS PQPSPTISIP VTPAPVPKPS
     PSPTPKPTVP PQISPTPQPS NTVPVIPPPE NPSAETEPNL PAPPVGEKPI DPEQN