ID   SPKI_SYNY3              Reviewed;         585 AA.
AC   P73627;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 126.
DE   RecName: Full=Probable serine/threonine-protein kinase I {ECO:0000305};
DE            EC=2.7.11.- {ECO:0000305};
DE   AltName: Full=Ser/Thr protein kinase SpkI {ECO:0000303|PubMed:35629380};
GN   Name=spkI {ECO:0000303|PubMed:35629380};
GN   OrderedLocusNames=sll1770 {ECO:0000312|EMBL:BAA17672.1};
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:BAA17672.1}
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=35629380; DOI=10.3390/life12050713;
RA   Wang X., Ge H., Zhang Y., Wang Y., Zhang P.;
RT   "Ser/Thr Protein Kinase SpkI Affects Photosynthetic Efficiency in
RT   Synechocystis sp. PCC 6803 upon Salt Stress.";
RL   Life 12:0-0(2022).
CC   -!- FUNCTION: Protein kinase involved in maintaining high-effective
CC       photosynthesis upon salt stress (PubMed:35629380). It may play a role
CC       in high-salt adaptation mechanisms (PubMed:35629380). It is involved in
CC       regulating redox state of the plastoquinone (PQ) pool under high salt
CC       condition and in photoprotection mechanisms (PubMed:35629380).
CC       {ECO:0000269|PubMed:35629380}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: When grown under control condition, the mutant
CC       has normal growth and photosynthesis and shows a significantly higher
CC       non-photochemical quenching (NPQ) capacity (PubMed:35629380). However,
CC       when grown under high salt condition, the mutant exhibits slower growth
CC       as well as decreased net photosynthesis and PSII activity
CC       (PubMed:35629380). {ECO:0000269|PubMed:35629380}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17672.1; -; Genomic_DNA.
DR   PIR; S77114; S77114.
DR   AlphaFoldDB; P73627; -.
DR   SMR; P73627; -.
DR   IntAct; P73627; 2.
DR   STRING; 1148.gene:10498539; -.
DR   PaxDb; 1148-gene:10498539; -.
DR   EnsemblBacteria; BAA17672; BAA17672; BAA17672.
DR   KEGG; syn:sll1770; -.
DR   eggNOG; COG0661; Bacteria.
DR   InParanoid; P73627; -.
DR   PhylomeDB; P73627; -.
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   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR063398; Sll1770-like_C.
DR   InterPro; IPR050154; UbiB_kinase.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF113; PROTEIN ACTIVITY OF BC1 COMPLEX KINASE 7, CHLOROPLASTIC; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   Pfam; PF30499; ABC1_cyano_C; 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..585
FT                   /note="Probable serine/threonine-protein kinase I"
FT                   /id="PRO_0000200733"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          154..522
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         160..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   585 AA;  67128 MW;  78D100CD9D2752DB CRC64;
     MSALSTKLEP TNSYSESLPP QRRSPLEAEG RYRWNRGNYS ITRRRIDIWG FVLTLLYQFW
     LNGKKWSYAG GYTEEKLQQR RRRQAKWIRE NLLSLGPTFI KVGQLFSTRS DLFPAEYVEE
     LSKLQDEVPA FSYEQAAGII EEELGKPIAK LYRSFDPVPL AAASLGQVHK AQLHTGEDVV
     VKVQRPGLKK LFTIDLAILK KIAQYFQNHP KWGRGRDWNG IYEECCKILW QETDYLREGR
     SADTFRRNFR GEDWVKVPRV YWRYTSTQIL TLEYLPGIKI SHYDALEAAG LERKELAQLG
     ARAYLFQLLN HGFFHADPHP GNLAVSPEAG ELIFYDFGMM GEITPDTKNK LMDTLFGVAE
     KNAERIVNSL VALGALKETE DMGPIRRSVQ FLLDNFMDKP FEEQSITKIS DDLYEIAYDQ
     PFRFPATFTF VMRAFSTLEG VGKGLDPDFN FMAVAQPFAL QIMNNSNGFN PAGNIMDELG
     RQAVQVGNSA LGLPRRIEDS LDRLDRGDIR VRVRSTETDR LLRRMGTMQM GTNYVLFTCA
     LVLSATLLFV NNYFMAAAVV LLMSLVPAFA LWRLLKRLER QDRMF
//