ID   SPKF_SYNY3              Reviewed;         495 AA.
AC   P73469;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Serine/threonine-protein kinase F;
DE            EC=2.7.11.1;
GN   Name=spkF; OrderedLocusNames=slr1225;
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; AB046601; BAB17037.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17509.1; -; Genomic_DNA.
DR   PIR; S77406; S77406.
DR   AlphaFoldDB; P73469; -.
DR   SMR; P73469; -.
DR   IntAct; P73469; 2.
DR   STRING; 1148.1652588; -.
DR   PaxDb; P73469; -.
DR   PRIDE; P73469; -.
DR   EnsemblBacteria; BAA17509; BAA17509; BAA17509.
DR   KEGG; syn:slr1225; -.
DR   eggNOG; COG0515; Bacteria.
DR   InParanoid; P73469; -.
DR   PhylomeDB; P73469; -.
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   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.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..495
FT                   /note="Serine/threonine-protein kinase F"
FT                   /id="PRO_0000171244"
FT   DOMAIN          46..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          316..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         52..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   495 AA;  53873 MW;  A92D94FECA3B4774 CRC64;
     MDLLCTRPGC ARLNSFPDLD NRNTLQTVQQ RFCTSCRMPL ILAGRYLPVK LLGQGGFGAA
     YLALDRFTPT MRFCVVKQFQ PSGNLNQEQL DLALSLFERE AVVLEKLGNR HDQIPDLFAY
     FPLLVDDPRT GKQDQFFYLV QEFINGQDLE KTVEKHGPLS EAEVRWVLTE MLKILSFVHG
     TGAIHRDIKP SNLMRDQEGK LYLLDFGAVK QATAGVGASN EGSTGIYSMG FAPPEQMAGN
     QVYPATDLYA LAVTCLYLLT GKTAQDLYDA YHNQWNWRSP GLKVSQPLAD VIDRLLLPTP
     KDRYASAEEV LAVLNGGKGN QGKAPPGATV STPQGTNTQI QPTPASSASP LTAPKTPGKI
     SQAVQNLPVL KVLFQGALTG SALVFWGIIA VSLFPQTNIS LGILGMVVAG IILAQFKRWL
     EVTEMLSLNT LTILALLAVP GLSRWPKIVE LATQLDFPVL VTVIIAAIAG AIAVVATIAL
     FLLILKLLFA VLTRV