ID SPKA_SYNY3 Reviewed; 521 AA. AC Q9FAB3; P73208; P73209; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Serine/threonine-protein kinase A; DE EC=2.7.11.1; GN Name=spkA; OrderedLocusNames=sll1574/sll1575; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=11160079; DOI=10.1128/jb.183.5.1505-1510.2001; RA Kamei A., Yuasa T., Orikawa K., Geng X.X., Ikeuchi M.; RT "A eukaryotic-type protein kinase, SpkA, is required for normal motility of RT the unicellular Cyanobacterium synechocystis sp. strain PCC 6803."; RL J. Bacteriol. 183:1505-1510(2001). 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 -!- FUNCTION: Protein kinase that regulates cellular motility via CC phosphorylation of membrane proteins. 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. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA17235.1; Type=Frameshift; Note=sll1574 and sll1575 have been merged into one gene.; Evidence={ECO:0000305}; CC Sequence=BAA17236.1; Type=Frameshift; Note=sll1574 and sll1575 have been merged into one gene.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB046597; BAB17033.1; -; Genomic_DNA. DR EMBL; BA000022; BAA17235.1; ALT_FRAME; Genomic_DNA. DR EMBL; BA000022; BAA17236.1; ALT_FRAME; Genomic_DNA. DR PIR; S75321; S75321. DR PIR; S75322; S75322. DR AlphaFoldDB; Q9FAB3; -. DR SMR; Q9FAB3; -. DR IntAct; Q9FAB3; 3. DR STRING; 1148.gene:10498098; -. DR PaxDb; 1148-1652312; -. DR EnsemblBacteria; BAA17235; BAA17235; BAA17235. DR EnsemblBacteria; BAA17236; BAA17236; BAA17236. DR KEGG; syn:sll1574; -. DR KEGG; syn:sll1575; -. DR eggNOG; COG0515; Bacteria. DR InParanoid; Q9FAB3; -. DR PhylomeDB; Q9FAB3; -. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..521 FT /note="Serine/threonine-protein kinase A" FT /id="PRO_0000171239" FT DOMAIN 15..289 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 148 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 21..29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 45 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 521 AA; 58875 MW; 5FEC16F80D369C91 CRC64; MTPDSRHRRL LANRYQLVEL VGSGAMGQVY RAEDKLLGGV TVAVKFLSQA LLNPRMKERF EREATISALL GEKSIHIVRV RDYGLDEKEI PFYVMEYLQG ENISDVIKYR PLKVERFLKI ARQICFGLDC AHKGIIYQGE ACPVVHRDIK PSNVLLVEDP ALGELVKILD FGIAKLVQAA EESKTQAFMG TLAYCSPEQM EGKELDSRSD IYSLGVMMYE MLTGEMPLFP DNSSFGGWYE AHHHTKPHPF SARYKIPASL EALVMNCLAK SPKGRPQSVD VIIRAIDAIE AEIKAPPISD TEKTQIAPHL LNTDMEATVV AQRGPGIVPE TRLPLVSELC KQLEWPSDKP KQKIVFPYVL NAAEGKLASL WVMLNQEDIL TRMSSIRYNQ FLLMTSPHPM VLWITVLYHR EYGPRWLPCY LDLKTRSGQS FAQMLGESGT YWLLFFALEN PTRCQHMLTA TVAPNQCKLL KEWAQTSQSM PGGKPQVTKR LLKQELDRLK PKIEAKLSQV KPSFNKEVSG L //