CSK_PHATC
ID CSK_PHATC Reviewed; 583 AA.
AC B7GDS0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Chloroplast sensor kinase, chloroplastic {ECO:0000303|PubMed:31925322};
DE EC=2.7.13.3;
DE Flags: Precursor;
GN Name=CSK {ECO:0000303|PubMed:31925322};
GN ORFNames=PHATRDRAFT_41268 {ECO:0000312|EMBL:EEC43310.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1;
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS, AND TRANSIT PEPTIDE.
RX PubMed=25438865; DOI=10.1111/tpj.12734;
RA Gruber A., Rocap G., Kroth P.G., Armbrust E.V., Mock T.;
RT "Plastid proteome prediction for diatoms and other algae with secondary
RT plastids of the red lineage.";
RL Plant J. 81:519-528(2015).
RN [4]
RP FUNCTION, AND COFACTOR.
RX PubMed=31925322; DOI=10.1038/s42003-019-0728-4;
RA Ibrahim I.M., Wu H., Ezhov R., Kayanja G.E., Zakharov S.D., Du Y.,
RA Tao W.A., Pushkar Y., Cramer W.A., Puthiyaveetil S.;
RT "An evolutionarily conserved iron-sulfur cluster underlies redox sensory
RT function of the Chloroplast Sensor Kinase.";
RL Commun. Biol. 3:13-13(2020).
CC -!- FUNCTION: Sensor kinase that senses the plastoquinone (PQ) redox state
CC involved in stoichiometry adjustment of both photosystems (e.g. long-
CC term adaptation via transcriptional regulation of reaction center genes
CC of photosystems I and II) and state transitions (e.g. short-term
CC adaptation involving reversible post-translational phosphorylation of
CC light-harvesting complex II, LHC II), thus linking photosynthesis with
CC gene expression in chloroplasts (By similarity). Reduced PQ suppresses
CC its autophosphorylation activity (Probable).
CC {ECO:0000250|UniProtKB:F4HVG8, ECO:0000305|PubMed:31925322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:F4HVG8};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:31925322};
CC Note=The 3Fe-4S cluster is redox-responsive, probably binds 1 cluster
CC per monomer. {ECO:0000269|PubMed:31925322};
CC -!- SUBUNIT: Oligomerizes. {ECO:0000250|UniProtKB:F4HVG8}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:25438865}. Note=In this organism the plastid is the
CC result of a secondary endosymbiosis event, and is found within the
CC endomembrane system, necessitating a complex targeting process.
CC {ECO:0000305|PubMed:25438865}.
CC -!- PTM: Autophosphorylates, possibly on His-292.
CC {ECO:0000305|PubMed:31925322}.
CC -!- MISCELLANEOUS: Probably has a bipartite transit peptide. The signal to
CC cross the ER endomembrane system is probably residues 1-31 while the
CC transit peptide is probably residues 32-50.
CC {ECO:0000305|PubMed:25438865}.
CC -!- SIMILARITY: Belongs to the chloroplast sensor kinase protein family.
CC {ECO:0000305|PubMed:31925322}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC43310.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:25438865};
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DR EMBL; CM000630; EEC43310.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002185178.1; XM_002185142.1.
DR AlphaFoldDB; B7GDS0; -.
DR GeneID; 7198991; -.
DR KEGG; pti:PHATRDRAFT_41268; -.
DR eggNOG; ENOG502S572; Eukaryota.
DR HOGENOM; CLU_493029_0_0_1; -.
DR InParanoid; B7GDS0; -.
DR OrthoDB; 1534881at2759; -.
DR Proteomes; UP000000759; Chromosome 28.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR Pfam; PF02518; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 3: Inferred from homology;
KW 3Fe-4S; Chloroplast; Iron; Iron-sulfur; Kinase; Metal-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:25438865"
FT CHAIN 51..583
FT /note="Chloroplast sensor kinase, chloroplastic"
FT /id="PRO_0000453139"
FT DOMAIN 447..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 97..277
FT /note="GAF"
FT /evidence="ECO:0000305|PubMed:31925322"
FT REGION 412..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305|PubMed:31925322"
FT MOD_RES 292
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 583 AA; 63168 MW; 79DD1F452F113BE8 CRC64;
MSSIYLHGLS RRRRIGSVIV AIYMLDSCGA FLSASGSGRY PGFSYRGLSV VTENIRSIHS
SRRLKLTVNA TNKEMYERQD SIHTLPLSPI PVMPSQLFQE LALSQLELLA NSIPCADRPG
VSKIKTMALY LPQENVNTGQ LEFLPAIHYP HPSRERVFIA NEAASGVAPA LPRTLTTLPG
FAHATSLLPG YPMVSGGSEA SVGVVEEVIC DLTSGAAALS VPLFSGSRTV GVLLVSPSIS
KRRKGSAWTK EDREQVGRAG KSLSLALSMD TERAALQMQN DRAARALSDS LHQIKNPLQA
MRTYGKLLQR RIADLGLLSN EGMTPQLLEM AEHLLVQSDR LADRLKPVDT IVDSLSERTP
FVLNPAAPTK TQDSLVSLAT PLVPWESETL EFARESKTSG ELVIFMPTKK VAASGSNGPS
NSTTSFSGNG SDVSTYTEDD GAGEMPSSLF SEMDLEMSFL SDVLDPVLAA FRAIAEDRGI
MFSHDDTEDL PGVTICPQAL QEALINVIDN AFTYVFLPKP GSRFGPNPSA EVRIRLVQNS
KGSDAGVTIL VEDNGPGIPA ETRDQIFDRG KDQALDWTLR KHW
