ID   SPKK_SYNY3              Reviewed;         566 AA.
AC   P73121;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Probable serine/threonine-protein kinase K {ECO:0000305};
DE            EC=2.7.11.- {ECO:0000305};
GN   Name=spkK {ECO:0000303|PubMed:21551175};
GN   OrderedLocusNames=slr1919 {ECO:0000312|EMBL:BAA17147.1};
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1] {ECO:0000312|EMBL:BAA17147.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / 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).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27184 / PCC 6803;
RX   PubMed=21551175; DOI=10.1093/dnares/dsr006;
RA   Zorina A., Stepanchenko N., Novikova G.V., Sinetova M., Panichkin V.B.,
RA   Moshkov I.E., Zinchenko V.V., Shestakov S.V., Suzuki I., Murata N.,
RA   Los D.A.;
RT   "Eukaryotic-like Ser/Thr protein kinases SpkC/F/K are involved in
RT   phosphorylation of GroES in the Cyanobacterium synechocystis.";
RL   DNA Res. 18:137-151(2011).
CC   -!- FUNCTION: Protein kinase involved, together with SpkC and SpkF, in the
CC       phosphorylation of the small chaperonin GroES (PubMed:21551175). These
CC       three kinases are probably organized in a sequential order or a cascade
CC       and they work one after another to finally phosphorylate GroES
CC       (PubMed:21551175). {ECO:0000269|PubMed:21551175}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of either spkC, spkF or spkK leads
CC       to inability of cells to phosphorylate GroES.
CC       {ECO:0000269|PubMed:21551175}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {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; BA000022; BAA17147.1; -; Genomic_DNA.
DR   PIR; S75233; S75233.
DR   AlphaFoldDB; P73121; -.
DR   SMR; P73121; -.
DR   IntAct; P73121; 2.
DR   STRING; 1148.gene:10498008; -.
DR   PaxDb; 1148-gene:10498008; -.
DR   EnsemblBacteria; BAA17147; BAA17147; BAA17147.
DR   KEGG; syn:slr1919; -.
DR   eggNOG; COG0661; Bacteria.
DR   InParanoid; P73121; -.
DR   PhylomeDB; P73121; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR050154; UbiB_kinase.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF128; UBIB DOMAIN CONTAINING KINASE; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   Pfam; PF27536; UbiB_helical; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..566
FT                   /note="Probable serine/threonine-protein kinase K"
FT                   /id="PRO_0000200734"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          139..469
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        302
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         145..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   566 AA;  65079 MW;  0C50CC04509FDCB3 CRC64;
     MPNPKPLPPQ SELDNIRRYN AQAIANYYRR RPWKVLWRAL EVVWSFGFFL TCLLWDQWTG
     QVEYYKRQRA EDLRELLTKL GPTFIKVGQA LSTRPDLVRR DFLEELIKLQ DQLPPFDNDL
     AFQLMEEQLG MKVDEAYREI SAHPVAAASL GQVYRAMLFS GEEVAVKVQR PNLRPRLSLD
     LYLMRLGAQK FGRFLPLNLG HDLTLIVDEF GIKLFEEIDY LNEGRNAEKF AENFHGDAEV
     KVPCIYWQYS NQKVLTLEWI QGFKLTDTDK IRAAGLDPSD IIRIGVTSGL RQLLEHGFFH
     ADPHPGNLFA TLDGRMAYID FGMMDQLEPG TKETIASSIV QLINKDYLAL TEDFIALGFL
     APNTDITPII PALENVFGSA IGQSVQDFNF KTITDDFSEL MYDYPFRVPA KFALIIRSLV
     TQEGLALSLD PNFKIVEVAY PYVARRLLTG ESPQLRRQLI DVLFKNGKFQ WQRLENMLSI
     ARSDTKFDLL PTAQLGLQFL FSEEGLYLRR QILLALTEDD RLHTDEVQRI WGLVKDDFKP
     QELVNVAWNA VREFSLAGVS TILPQR
//