ID   Q2JXA0_SYNJA            Unreviewed;       650 AA.
AC   Q2JXA0;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=CYA_0373 {ECO:0000313|EMBL:ABC98592.1};
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321327 {ECO:0000313|EMBL:ABC98592.1, ECO:0000313|Proteomes:UP000008818};
RN   [1] {ECO:0000313|EMBL:ABC98592.1, ECO:0000313|Proteomes:UP000008818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABC98592.1,
RC   ECO:0000313|Proteomes:UP000008818};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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|ARBA:ARBA00001433};
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|ARBA:ARBA00000775};
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DR   EMBL; CP000239; ABC98592.1; -; Genomic_DNA.
DR   RefSeq; WP_011429281.1; NC_007775.1.
DR   AlphaFoldDB; Q2JXA0; -.
DR   STRING; 321327.CYA_0373; -.
DR   KEGG; cya:CYA_0373; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_417915_0_0_3; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000008818; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABC98592.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABC98592.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABC98592.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        449..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        508..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        547..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        579..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        607..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..306
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          377..410
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          423..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  71512 MW;  B98D67CA4ABE0F5D CRC64;
     MNQRLIGQLI GNRYRLTHHI SEGGYGNVFE AVDTQLNDEP VAVKLLRPPP PDMEPEYYQQ
     LQQRFLDEAR VSALLGEHPN IVQVRSYGLY QNQPYLVMEY LKAKPYTGQG LDYVLAREGP
     LHPERVVNLA LQICSALHHA HNFHMDLGKH SIRGVIHRDI KPSNIFVQKG PDGKERVKLL
     DFGISKLMGE TSRGLTQTGY FLGTMVYASP EQMRGEKLDG RSDIYSLGVV LYELLTGALP
     FEPETDTLQG WYHVHNFQKP RPFQDHPLPH PIPEALEKVV LRCLEKDPAL RPATMEELAQ
     QLRAVYGDKI PPPPQKAPLQ RIPAGFGQQA TQQSRAAPVS EAEEEELQRA VRLIEAGEYK
     MAVHLLNKLI QSAPNEARYY LYRGLAHQRQ GHWGLAQMDY QGVLRLEPGN PSAEQGLREV
     EQQVGQEQVS PHQKPTLPTS GKPRQRKGLA LGWLLANWAA AGIGYLGLGA AAPLLAALGS
     LQGAVAGAGL GLGMGLLQWA VLRRQVSWRW VAATLLATAL GWVAADTLEA GMATFAFDPR
     DPWLQNALQA MASPLRGLLV GLGVGGLQGI LLSRHGKVAW AWVLAAGVEG GGAALLIHWL
     LAGSALSRWL LLLAGLLAHT RPLSALVLAN LNWRRIPAVQ NCQQAKQQAA
//