ID RSH1C_ARATH Reviewed; 884 AA.
AC F4JHA2; Q0WUY0; Q9M112; Q9M5P7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 85.
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; OrderedLocusNames=At4g02260; ORFNames=T2H3.10;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 1).
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 [4]
RP INTERACTION WITH RPP5.
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).
RN [5]
RP INTERACTION WITH RPP4 AND RPP5.
RX PubMed=11846877; DOI=10.1046/j.0960-7412.2001.01229.x;
RA van der Biezen E.A., Freddie C.T., Kahn K., Parker J.E., Jones J.D.;
RT "Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR
RT genes and confers downy mildew resistance through multiple signalling
RT components.";
RL Plant J. 29:439-451(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, 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: May be involved in a rapid plant ppGpp (guanosine 3'-
CC diphosphate 5'-diphosphate)-mediated response to pathogens and other
CC stresses (By similarity). Unable to functionally complement E.coli relA
CC mutants. {ECO:0000250, 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 -!- SUBUNIT: Interacts with RPP4 (PubMed:11846877). Interacts with RPP5
CC (PubMed:10725385, PubMed:11846877). {ECO:0000269|PubMed:10725385,
CC ECO:0000269|PubMed:11846877}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18535838}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JHA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JHA2-2; Sequence=VSP_055308;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, shoots, cotyledons,
CC rosette leaves, sepals and pistils. {ECO:0000269|PubMed:18535838}.
CC -!- INDUCTION: Circadian-regulation with a peak at dusk. Down-regulated by
CC wounding and 12-oxo-phytodienoic acid (OPDA).
CC {ECO:0000269|PubMed:18535838}.
CC -!- MISCELLANEOUS: In the ecotype Landsberg erecta, RSH1 (AC P0DKG8) has
CC been shown to interact with RPP5 (AC O04264).
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB80719.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161494; CAB80719.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82147.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82148.1; -; Genomic_DNA.
DR EMBL; AK227003; BAE99068.1; -; mRNA.
DR PIR; H85028; H85028.
DR RefSeq; NP_567226.1; NM_116459.4. [F4JHA2-2]
DR RefSeq; NP_849287.2; NM_178956.4. [F4JHA2-1]
DR AlphaFoldDB; F4JHA2; -.
DR SMR; F4JHA2; -.
DR BioGRID; 13387; 1.
DR STRING; 3702.F4JHA2; -.
DR PaxDb; 3702-AT4G02260-1; -.
DR ProteomicsDB; 228061; -. [F4JHA2-1]
DR EnsemblPlants; AT4G02260.1; AT4G02260.1; AT4G02260. [F4JHA2-1]
DR EnsemblPlants; AT4G02260.2; AT4G02260.2; AT4G02260. [F4JHA2-2]
DR GeneID; 828096; -.
DR Gramene; AT4G02260.1; AT4G02260.1; AT4G02260. [F4JHA2-1]
DR Gramene; AT4G02260.2; AT4G02260.2; AT4G02260. [F4JHA2-2]
DR KEGG; ath:AT4G02260; -.
DR Araport; AT4G02260; -.
DR TAIR; AT4G02260; RSH1.
DR eggNOG; KOG1157; Eukaryota.
DR InParanoid; F4JHA2; -.
DR OrthoDB; 1396at2759; -.
DR PRO; PR:F4JHA2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JHA2; baseline and differential.
DR Genevisible; F4JHA2; 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:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IMP:TAIR.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IDA: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 CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 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 PANTHER; PTHR43061; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43061:SF1; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF13328; HD_4; 1.
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; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; GTP-binding; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Stress response;
KW Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..884
FT /note="Putative GTP diphosphokinase RSH1, chloroplastic"
FT /id="PRO_0000429844"
FT DOMAIN 172..279
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 563..626
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 797..868
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 711..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055308"
FT CONFLICT 491
FT /note="G -> D (in Ref. 3; BAE99068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 884 AA; 98690 MW; 91A6726EBA984FDF 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 IAQQLRIVVK PKPSVGVGPL
CSPQQICYHV LGLVHEIWKP IPRTVKDYIA TPKPNGYQSL HTTVIPFLYE SMFRLEVQIR
TEEMDLIAER GIAVYYNGKS LSTGLVGNAV PLGRNSRGKT GCLNNADFAL RVGWLNAIRE
WQEEFVGNMS SREFVDTITR DLLGSRVFVF TPKGEIKNLP KGATVVDYAY LIHTEIGNKM
VAAKVNGNLV SPTHVLENAE VVEIVTYNAL SSKSAFQRHK QWLQHAKTRS ARHKIMRFLR
EQAAQCAAEI TQDQVNDFVA DSDSDVEDLT EDSRKSLQWW EKILVNVKQF QSQDKSRDTT
PAPQNGSVWA PKVNGKHNKA IKNSSSDEPE FLLPGDGIAR ILPANIPAYK EVLPGLDSWR
DSKIATWHHL EGQSIEWLCV VSMDRKGIIA EVTTVLAAEG IALCSCVAEI DRGRGLAVML
FQIEANIESL VSVCAKVDLV LGVLGWSSGC SWPRSTENAQ VLEC
//
