ID   RSH1L_ARATH             Reviewed;         883 AA.
AC   P0DKG8; Q9M5P7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Putative GTP diphosphokinase RSH1, chloroplastic;
DE            EC=2.7.6.5;
DE   AltName: Full=RelA/SpoT homolog 1;
DE            Short=AtRSH1;
DE   AltName: Full=ppGpp synthetase RSH1;
DE   Flags: Precursor;
GN   Name=RSH1;
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 [MRNA], FUNCTION, AND INTERACTION WITH RPP5.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10725385; DOI=10.1073/pnas.97.7.3747;
RA   van der Biezen E.A., Sun J., Coleman M.J., Bibb M.J., Jones J.D.;
RT   "Arabidopsis RelA/SpoT homologs implicate (p)ppGpp in plant signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3747-3752(2000).
CC   -!- FUNCTION: May be involved in a rapid plant ppGpp (guanosine 3'-
CC       diphosphate 5'-diphosphate)-mediated response to pathogens and other
CC       stresses. {ECO:0000269|PubMed:10725385}.
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   -!- SUBUNIT: Interacts with RPP5. {ECO:0000269|PubMed:10725385}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AF225702; AAF37281.1; -; mRNA.
DR   RefSeq; NP_567226.1; NM_116459.4.
DR   AlphaFoldDB; P0DKG8; -.
DR   SMR; P0DKG8; -.
DR   BioGRID; 13387; 1.
DR   PRIDE; P0DKG8; -.
DR   EnsemblPlants; AT4G02260.2; AT4G02260.2; AT4G02260.
DR   GeneID; 828096; -.
DR   Gramene; AT4G02260.2; AT4G02260.2; AT4G02260.
DR   KEGG; ath:AT4G02260; -.
DR   PhylomeDB; P0DKG8; -.
DR   PRO; PR:P0DKG8; -.
DR   ExpressionAtlas; P0DKG8; baseline and differential.
DR   Genevisible; P0DKG8; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chloroplast; GTP-binding; Kinase; Nucleotide-binding; Plastid;
KW   Stress response; Transferase; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..883
FT                   /note="Putative GTP diphosphokinase RSH1, chloroplastic"
FT                   /id="PRO_0000429845"
FT   DOMAIN          172..279
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          562..625
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          796..867
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          710..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  98562 MW;  3A6187EEA4B5E89F CRC64;
     MTSASSMSVS VECVNICNLT KGDGNARSDC SALSCAWKAP RALTGFLAST AHPPVCSVYS
     CGRNGRKSRM KACAWQRYEY EVGFSEAPYF VNVRNILKSR LSCGGHKRWE LYCVSAESSS
     GASSDVTVET LWEDLFPSIS YLPRKELEFV QKGLKLAFEA HHGQKRRSGE PFIIHPVAVA
     RILGELELDW ESIVAGLLHD TVEDTNFITF EKIEEEFGAT VRHIVEGETK VSKLGKLKCK
     TESETIQDVK ADDLRQMFLA MTDEVRVIIV KLADRLHNMR TLCHMPPHKQ SSIAGETLQV
     FAPLAKLLGM YSIKSELENL SFMYVSAEDY DRVTSRIANL YKEHEKELTE ANRILVKKIE
     DDQFLDLVTV NTDVRSVCKE TYSIYKAALK SKGSINDYNQ IAQLRIVVKP KPSVGVGPLC
     SPQQICYHVL GLVHEIWKPI PRTVKDYIAT PKPNGYQSLH TTVIPFLYES MFRLEVQIRT
     EEMDLIAERG IAVYYNGKSL STGLVGNAVP LGRNSRGKTG CLNNADFALR VGWLNAIREW
     QEEFVGNMSS REFVDTITRD LLGSRVFVFT PKGEIKNLPK GATVVDYAYL IHTEIGNKMV
     AAKVNGNLVS PTHVLENAEV VEIVTYNALS SKSAFQRHKQ WLQHAKTRSA RHKIMRFLRE
     QAAQCAAEIT QDQVNDFVAD SDSDVEDLTE DSRKSLQWWE KILVNVKQFQ SQDKSRDTTP
     APQNGSVWAP KVNGKHNKAI KNSSSDEPEF LLPGDGIARI LPANIPAYKE VLPGLDSWRD
     SKIATWHHLE GQSIEWLCVV SMDRKGIIAE VTTVLAAEGI ALCSCVAEID RGRGLAVMLF
     QIEANIESLV SVCAKVDLVL GVLGWSSGCS WPRSTENAQV LEC