STT7_CHLRE
ID STT7_CHLRE Reviewed; 754 AA.
AC Q84V18;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Serine/threonine-protein kinase stt7, chloroplastic;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=STT7;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12624266; DOI=10.1126/science.1081397;
RA Depege N., Bellafiore S., Rochaix J.-D.;
RT "Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state
RT transition in Chlamydomonas.";
RL Science 299:1572-1575(2003).
RN [2]
RP IDENTIFICATION.
RX PubMed=10521495; DOI=10.1074/jbc.274.43.30987;
RA Fleischmann M.M., Ravanel S., Delosme R., Olive J., Zito F., Wollman F.-A.,
RA Rochaix J.-D.;
RT "Isolation and characterization of photoautotrophic mutants of
RT Chlamydomonas reinhardtii deficient in state transition.";
RL J. Biol. Chem. 274:30987-30994(1999).
CC -!- FUNCTION: Serine/threonine protein kinase required for state transition
CC by phosphorylating light-harvesting complex II outer antennae (LCHII).
CC State transition plays a central role in response to environmental
CC changes and allows to adjust to changing light conditions via the
CC redistribution of light excitation energy between photosystem II (PSII)
CC and photosystem I (PSI). {ECO:0000269|PubMed:12624266}.
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 -!- 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;
CC -!- INTERACTION:
CC Q84V18; P23577: petA; NbExp=5; IntAct=EBI-15762546, EBI-9013553;
CC Q84V18; A8J9Y1: PETC; NbExp=4; IntAct=EBI-15762546, EBI-15762582;
CC Q84V18; P12154: psaA; NbExp=4; IntAct=EBI-15762546, EBI-601796;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:12624266}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY220122; AAO63768.1; -; mRNA.
DR AlphaFoldDB; Q84V18; -.
DR SMR; Q84V18; -.
DR DIP; DIP-48400N; -.
DR IntAct; Q84V18; 6.
DR EnsemblPlants; PNW87374; PNW87374; CHLRE_02g120250v5.
DR Gramene; PNW87374; PNW87374; CHLRE_02g120250v5.
DR OMA; PANCIVS; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044803; STT7-like.
DR PANTHER; PTHR46699; PTHR46699; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Kinase; Membrane; Nucleotide-binding; Plastid;
KW Serine/threonine-protein kinase; Thylakoid; Transferase; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..754
FT /note="Serine/threonine-protein kinase stt7, chloroplastic"
FT /id="PRO_0000024387"
FT DOMAIN 139..482
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 660..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 145..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 754 AA; 80745 MW; 1BE8E69FAB7D6728 CRC64;
MALAQRQVSC RIERSTGAST SQPVGSCLLV QRRPGQRRGV PARATPEFID ALSALVPNLP
LEQIAAPCQV MKCGDIVYRS TLDPSLYNEA GFDEKTVALL APVLAYLFLP PGVLPGAIDY
YIRAPLKRKQ TKAIDKNDIV LGKRLGTGGF GTVFKGELKE EGGVKTSIII KKAKEFGEAE
VWMNERMSRV AGHHVAEFVT AFDESLNVPL PAAAGKRAAP VQPTSPLDAN SIWLVWVYEG
DNTLSSLMER REWPYNLEPL LFGRELRAPR GPVRELVTIK EAFRQLVQAV AACHSVGIVH
RDIKPANCIV SERDKKIKLI DLGAAADLRI GINYVPNEYL LDPRYAPPQQ YIMSTQTPKP
PPKPVAAFLS PILWTMEKPD RFDMYSCGIT LLQMVFGHLR NDNALIAFNK RLQELKWDLP
AWRREEEAKL PSAKGALAES LEAGFEALDA DGGAGWDLLM RLLAYKPTDR PSAAAVLAHP
WLTSAPGRTA SLQHSLSGSF EATVSTAAAA TSTALTAAGK SLGQAAKDAG LASMEEAILK
VNQGALTEAQ LMEELGLQEP APVAPREGSQ TIAWWQERQN ELKARLVERR EAMSESDPYG
AAPSAMQVGS AINNARGGKG AKPTTPVKPT GPMAAAGAAA AAAAAAARVE AKVKVPNILG
VKKPASGGGS NGRANGNGNG KAAPAKAANG NGSGNGNTNG NGNGAKQQLF GGLLGRKQQP
VEEVQEEPEE EVEPEQETAS KKERAFNLLG VFRR
