ID K9XYA9_STAC7 Unreviewed; 538 AA.
AC K9XYA9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Serine/threonine-protein kinase B {ECO:0000256|PIRNR:PIRNR000647};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000647};
GN OrderedLocusNames=Sta7437_4046 {ECO:0000313|EMBL:AFZ37523.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ37523.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 Evidence={ECO:0000256|PIRNR:PIRNR000647};
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; Evidence={ECO:0000256|PIRNR:PIRNR000647};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000647}.
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DR EMBL; CP003653; AFZ37523.1; -; Genomic_DNA.
DR RefSeq; WP_015195181.1; NC_019748.1.
DR AlphaFoldDB; K9XYA9; -.
DR STRING; 111780.Sta7437_4046; -.
DR KEGG; scs:Sta7437_4046; -.
DR PATRIC; fig|111780.3.peg.4196; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1357; Bacteria.
DR HOGENOM; CLU_000288_135_5_3; -.
DR OrthoDB; 428645at2; -.
DR Proteomes; UP000010473; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001646; 5peptide_repeat.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016252; Ser/Thr_kinase_SpkB.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00805; Pentapeptide; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000647; Ser/Thr_PK_SpkB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|PIRNR:PIRNR000647, ECO:0000313|EMBL:AFZ37523.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000647,
KW ECO:0000313|EMBL:AFZ37523.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR000647, ECO:0000313|EMBL:AFZ37523.1}.
FT DOMAIN 34..300
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 538 AA; 59720 MW; 6187637C4B1EABFD CRC64;
MSYCLNPSCP KPINNPKAKI CQACGSKLLL RDRYHLVKGL GKGGFGATFL AADISLPGNP
LCVIKQLRPN TDNPNFLSMA RQLFEREAKT LGRIGSHPQI PRLLDYFEDR KQFYLVQEFV
KGNNLQQEVK KHGLLNEEKV RQVLKEILVI LKDIHNQKVI HRDIKPANII RREIDDKLVL
IDFGVVKNQV NTVASDNNNT ALTAFAVGTP GFAPPEQLAM RPVYASDIYA LGVTCIYLLT
GKAPKNMDCD PLTGEINWDK YLNVSESFSE ILHTMLEVSV KNRYKTAEEA LQALDIENHL
DSLSESMISY SSGNIDPFSN SSSRGNRSTS RIADNIRSRH TSINPAAKRT IAGQDFKKTH
SNRTSFSRGT SIGKNSSDFK KSTSFGTSAY DLNRPVKLEA QALLDYYSTG RRDFNQKDLS
QQNLEKANLA GAHFHESKFI KTNLQGADLS GVDLSSADIR QALLRNANLC RAYLYSANLE
GADLRGADLS FTQFSGAKLK GANLCGANLS NANITEAQLK EAKTNWMTIL PNGRRGLW
//
