CRSH2_ORYSJ
ID CRSH2_ORYSJ Reviewed; 559 AA.
AC Q6ATB2; A0A0P0WIN5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=GTP diphosphokinase CRSH2, chloroplastic {ECO:0000305};
DE EC=2.7.6.5 {ECO:0000269|PubMed:17938177};
DE AltName: Full=Calcium-activated RelA/Spot homolog 2 {ECO:0000303|PubMed:17938177};
DE Short=OsCRSH2 {ECO:0000303|PubMed:17938177};
DE AltName: Full=ppGpp synthetase CRSH2 {ECO:0000303|PubMed:17938177};
DE Flags: Precursor;
GN Name=CRSH2 {ECO:0000303|PubMed:17938177};
GN OrderedLocusNames=Os05g0161500 {ECO:0000312|EMBL:BAS92406.1},
GN LOC_Os05g06920 {ECO:0000305};
GN ORFNames=OSJNBa0034O12.17 {ECO:0000312|EMBL:AAT93922.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, AND TISSUE
RP SPECIFICITY.
RX PubMed=17938177; DOI=10.1074/jbc.m703820200;
RA Tozawa Y., Nozawa A., Kanno T., Narisawa T., Masuda S., Kasai K.,
RA Nanamiya H.;
RT "Calcium-activated (p)ppGpp synthetase in chloroplasts of land plants.";
RL J. Biol. Chem. 282:35536-35545(2007).
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. May be involved in a rapid
CC plant ppGpp-mediated response to pathogens and other stresses.
CC {ECO:0000269|PubMed:17938177}.
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 Evidence={ECO:0000269|PubMed:17938177};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22090;
CC Evidence={ECO:0000269|PubMed:17938177};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000269|PubMed:17938177}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots. {ECO:0000269|PubMed:17938177}.
CC -!- DOMAIN: The calcium-binding sites of the 2 EF-hand domains are required
CC for enzyme activity. {ECO:0000305|PubMed:17938177}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AC137614; AAT93922.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16640.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92406.1; -; Genomic_DNA.
DR EMBL; AK058438; BAG86692.1; -; mRNA.
DR RefSeq; XP_015637728.1; XM_015782242.1.
DR AlphaFoldDB; Q6ATB2; -.
DR SMR; Q6ATB2; -.
DR STRING; 4530.OS05T0161500-01; -.
DR PaxDb; Q6ATB2; -.
DR PRIDE; Q6ATB2; -.
DR EnsemblPlants; Os05t0161500-01; Os05t0161500-01; Os05g0161500.
DR GeneID; 4337890; -.
DR Gramene; Os05t0161500-01; Os05t0161500-01; Os05g0161500.
DR KEGG; osa:4337890; -.
DR eggNOG; KOG1157; Eukaryota.
DR HOGENOM; CLU_022292_1_0_1; -.
DR InParanoid; Q6ATB2; -.
DR OMA; YRSLHIA; -.
DR OrthoDB; 505873at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6ATB2; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
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; cd00051; EFh; 1.
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 1: Evidence at protein 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..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..559
FT /note="GTP diphosphokinase CRSH2, chloroplastic"
FT /id="PRO_0000429855"
FT DOMAIN 87..187
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 449..484
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 486..518
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 559 AA; 60274 MW; C6877CE38B06FA93 CRC64;
MASAGGEVVV VDPAAAAVAP DVEHHAPAPR LTPAGSGGRL MAELLGVFNG LTERMGDDVA
TSSSWTLLFR ALKLALPALR DAAGGRSLAR ALIVAASLAD LQMDAEVISA GIVRQAMDAG
AVAMADAEAQ LGPGAAALLL ESLDVKNAPS RVDVADEEAA SAVRNRILSG YDVRAVILEL
AIRLDAMKHL DGVPKHQQRT TSLEVLKVFA PLAHAVGAGA LSKELEDLSF WRLYPQAYAQ
VDQWLSGQED DCKRVLATCK DDLLQALAAD DELRHTVAGF DVKGRYKSRF SAMKKLVKDG
RRPEDVHDIL GMRVILDHRA GAGDGHRACI RTHEVIKGMW KDVPARTKDY IARPKGDGYR
SLHIAVDMSE PGPEGKKRPL MEVQIRTKEM NDAAVFGHAL YKGCLADPEE AKRLKDIMLA
AAEVAAQHLR DEPATGDQTG VPAAAAAAAS AGNIERAFRL LDKNGDGRIS MEELTELMED
LGAGGKDAEE LMRLLDDNND GSLSSDEFAL FQKRVELKAK LEDKDDEYKE ILRQKLQKVD
DTGLIHVYRK NLSDKLVSG
