CRSH_ARATH
ID CRSH_ARATH Reviewed; 583 AA.
AC Q84R11; Q9LUQ0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable GTP diphosphokinase CRSH, chloroplastic;
DE EC=2.7.6.5;
DE AltName: Full=Calcium-activated RelA/Spot homolog;
DE Short=AtCRSH;
DE AltName: Full=ppGpp synthetase CRSH;
DE Flags: Precursor;
GN Name=CRSH; OrderedLocusNames=At3g17470; ORFNames=MKP6.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18535838; DOI=10.1007/s00425-008-0758-5;
RA Mizusawa K., Masuda S., Ohta H.;
RT "Expression profiling of four RelA/SpoT-like proteins, homologues of
RT bacterial stringent factors, in Arabidopsis thaliana.";
RL Planta 228:553-562(2008).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18178586; DOI=10.1093/pcp/pcm177;
RA Masuda S., Mizusawa K., Narisawa T., Tozawa Y., Ohta H., Takamiya K.;
RT "The bacterial stringent response, conserved in chloroplasts, controls
RT plant fertilization.";
RL Plant Cell Physiol. 49:135-141(2008).
CC -!- FUNCTION: Possesses calcium-dependent ppGpp (guanosine 3'-diphosphate
CC 5'-diphosphate) synthetase activity in vitro and is able to
CC functionally complement E.coli relA mutants. Plays an important role in
CC the timing adjustment of pistil and pollen maturation required for
CC successful pollination. May be involved in a rapid plant ppGpp-mediated
CC response to pathogens and other stresses. {ECO:0000269|PubMed:18178586,
CC ECO:0000269|PubMed:18535838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000269|PubMed:18178586}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18178586}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots, cotyledons, rosette and
CC cauline leaves, stems, sepals, pistils and siliques.
CC {ECO:0000269|PubMed:18178586, ECO:0000269|PubMed:18535838}.
CC -!- INDUCTION: Circadian-regulation with a peak at midnight.
CC {ECO:0000269|PubMed:18535838}.
CC -!- DOMAIN: The calcium-binding sites of the 2 EF-hand domains are required
CC for enzyme activity.
CC -!- MISCELLANEOUS: Plants silencing CRSH have abnormally small siliques
CC with few seeds, due to altered timing of pistil and pollen maturation
CC and unsuccessful pollination. {ECO:0000305|PubMed:18178586}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022219; BAB02036.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75958.1; -; Genomic_DNA.
DR EMBL; BT006180; AAP04163.1; -; mRNA.
DR EMBL; AK228656; BAF00563.1; -; mRNA.
DR RefSeq; NP_188374.2; NM_112627.4.
DR AlphaFoldDB; Q84R11; -.
DR SMR; Q84R11; -.
DR STRING; 3702.AT3G17470.1; -.
DR PaxDb; Q84R11; -.
DR PRIDE; Q84R11; -.
DR ProteomicsDB; 224511; -.
DR EnsemblPlants; AT3G17470.1; AT3G17470.1; AT3G17470.
DR GeneID; 821012; -.
DR Gramene; AT3G17470.1; AT3G17470.1; AT3G17470.
DR KEGG; ath:AT3G17470; -.
DR Araport; AT3G17470; -.
DR TAIR; locus:2090487; AT3G17470.
DR eggNOG; KOG1157; Eukaryota.
DR HOGENOM; CLU_022292_1_0_1; -.
DR InParanoid; Q84R11; -.
DR PhylomeDB; Q84R11; -.
DR BioCyc; ARA:AT3G17470-MON; -.
DR PRO; PR:Q84R11; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84R11; baseline and differential.
DR Genevisible; Q84R11; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51831; HD; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Chloroplast; GTP-binding; Kinase; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Repeat; Stress response;
KW Transferase; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..583
FT /note="Probable GTP diphosphokinase CRSH, chloroplastic"
FT /id="PRO_0000429853"
FT DOMAIN 112..212
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 470..505
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 507..539
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 528
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 309
FT /note="Required for ppGpp synthetase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 583 AA; 66578 MW; A01B59A2BEDE4CDB CRC64;
MSVIRPSPIP IPRCRSQVLH RRLYSIQLIQ RRRRRWNPRS EVEDTAIEST ARSPEAAGGK
MVVELVGAFN EVTERMNSVW LSTSSSRLLF KALKLSIPIL QSLPLASDGR SPLSKALSLS
IILADLQMDA EVISASILSE VVDANAISIY EVRDHIGTGT AHLLHEIFRV KNIPFKVDVL
DDETAASLRK FYLTYYDIRA VIMDLVSKLD EMRHLDHLPR YRQQILSLEV LKIYSPLAHA
VGANHLSLEL EDISFRYLFP CSYIYLDSWL RGHENGSKPL IDVYKEQLHR SLKDDLVLAE
MVNDVYIKGR YKSRYSMMKK LLRDGRKPEE VNDVLGLRVI LMPNSVVNDV EVGEKACYRT
SEIIRSLWKE IPHRTKDYIA RPKENGYRSL HMAVDVSDSD QIRPLMEIQI RTMDMDGSAN
AGTASHSLYK GGLTDPKEAK RLKAIMLAAA DLAAIRLKDI SSNKHQSFKT TTNQRDRVFC
LLDKNGDGMI SIEELMEVME ELGAPGEDAE EMMQLLDSNS DGSLSSDEFD TFQKQVEFMR
KWEDRDNEYK SLLDEKLHDL PHQDTTGLIQ LYNKELEDRL STH
