SPKA_SYNY3
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 03-AUG-2022, entry version 127.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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};
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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; 1148.1652312; -.
DR PaxDb; Q9FAB3; -.
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: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; 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
