RSH2C_ARATH
ID RSH2C_ARATH Reviewed; 709 AA.
AC Q9LVJ3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable GTP diphosphokinase RSH2, chloroplastic;
DE EC=2.7.6.5;
DE AltName: Full=RelA/SpoT homolog 2;
DE Short=AtRSH2;
DE AltName: Full=ppGpp synthetase RSH2;
DE Flags: Precursor;
GN Name=RSH2; OrderedLocusNames=At3g14050; ORFNames=MDC16.19;
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 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).
CC -!- FUNCTION: Possesses ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC synthetase activity in vitro and is able to functionally complement
CC E.coli relA mutants. May be involved in a rapid plant ppGpp-mediated
CC response to pathogens and other stresses.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, shoots, cotyledons,
CC rosette and cauline leaves, stems, petals, sepals, stamens, pistils and
CC siliques. {ECO:0000269|PubMed:18535838}.
CC -!- INDUCTION: Circadian-regulation with a peak at noon. Induced by
CC wounding, salt stress, 12-oxo-phytodienoic acid (OPDA) and abscisic
CC acid (ABA). {ECO:0000269|PubMed:18535838}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AB019229; BAB02337.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75459.1; -; Genomic_DNA.
DR RefSeq; NP_188021.1; NM_112259.5.
DR AlphaFoldDB; Q9LVJ3; -.
DR SMR; Q9LVJ3; -.
DR BioGRID; 5953; 2.
DR STRING; 3702.AT3G14050.1; -.
DR iPTMnet; Q9LVJ3; -.
DR PaxDb; Q9LVJ3; -.
DR PRIDE; Q9LVJ3; -.
DR ProteomicsDB; 226784; -.
DR EnsemblPlants; AT3G14050.1; AT3G14050.1; AT3G14050.
DR GeneID; 820619; -.
DR Gramene; AT3G14050.1; AT3G14050.1; AT3G14050.
DR KEGG; ath:AT3G14050; -.
DR Araport; AT3G14050; -.
DR TAIR; locus:2088262; AT3G14050.
DR eggNOG; KOG1157; Eukaryota.
DR HOGENOM; CLU_012300_7_1_1; -.
DR InParanoid; Q9LVJ3; -.
DR OMA; HNEMSTM; -.
DR OrthoDB; 505873at2759; -.
DR PhylomeDB; Q9LVJ3; -.
DR BioCyc; ARA:AT3G14050-MON; -.
DR PRO; PR:Q9LVJ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVJ3; baseline and differential.
DR Genevisible; Q9LVJ3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51831; HD; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; GTP-binding; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..709
FT /note="Probable GTP diphosphokinase RSH2, chloroplastic"
FT /id="PRO_0000429847"
FT DOMAIN 233..337
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 709 AA; 79044 MW; 5B8B8DA70AF54BDD CRC64;
MVVATTIALY ASPPSSVCST PHQISCDLDL TSRSSSTSSS MASSPQKPIV GGLSSLFSSA
SVKSSSSSSC SYSTGVDEFS SLRYDRSDDL KDLSFSSSFG YSPAKFVNSF RRDHQSPISV
LHGPVSCSCS PPMRMSRDRN LDGSFRLGAS GLFNGFVRKA LGSCVDYEFG SDSVLVDELT
FPMEVDTIKP YARDLLRRAQ LRHKIFNDES VIKAFYEAEK AHRGQMRASR DPYLQHCVET
AMLLANIGAN STVVVAGLLH DTIDDSFMSY DYILRNFGAG VADLVEGVSK LSQLSKLARE
NNTACKTVEA DRLHTMFLAM ADARAVLIKL ADRLHNMKTL YALSPVKQQR FAKETLEIFA
PLANRLGIST WKVQLENLCF KHLYPNQHNE MSTMLEDSFD EAMITSAIEK LEQALKKAGI
SYHVLCGRHK SLYSIYSKML KKKLTVDEIH DIHGLRLIVD NEGDCYKALG VVHSLWSEVP
GKLKDYITHP KFNGYQSLHT VVMDNGTVPL EVQIRTQEMH LQAEFGFAAH WRYKEGGCKY
SSFVLQMVEW ARWVVTWHCE AMSKDRSSIS SSDSIKPPCK FPSHSEDCPA SYKPNSSQDG
PVYVIVIEND KMSVQEFPAS STVSDLLSRA GPGSSRWSMY GIPAKEELRP RLNQIPVSDL
KWKLKMGDVV ELTPTIPDES LTEYREEIQR MYDRGLAFSR PGTMVGWGS
