RSH2L_ARATH
ID RSH2L_ARATH Reviewed; 710 AA.
AC Q9M5P6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
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;
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].
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: Probable ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC synthetase that may be involved in a rapid plant ppGpp-mediated
CC response to pathogens and other stresses. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AF225703; AAF37282.1; -; mRNA.
DR AlphaFoldDB; Q9M5P6; -.
DR SMR; Q9M5P6; -.
DR ExpressionAtlas; Q9M5P6; baseline and differential.
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 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 Stress response; Transferase; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..710
FT /note="Probable GTP diphosphokinase RSH2, chloroplastic"
FT /id="PRO_0000429848"
FT DOMAIN 233..337
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 710 AA; 79207 MW; 7638AC41EDE0DDB4 CRC64;
MVVATTIALY ASPPSSVCST PHQISCDLDL TSRSSSTSSS MASSPQKPIV GGLSSLFSSA
SVKSSSSSSC SYSTAVDEFS SLRYDRSDDL KDLSFSSSFG YSPAKFVNSF RRDHQSPISV
LHGPVSCSCS PPMRMSRDRN LDGSFRLGAS RLFNGFVRKA LGSCVDYELG SDSGLVDELT
FPMEVDTIKP YARDLLRRAQ LRHKIFNDES VIKAFYEAEK AHRGQMRASR DPYLQHCVET
AMLLANIGAN STVVVAGLLH DTVDDSFMSY DYILRNFGAG VADLVEGVSK LSQLSKLARE
NNTACKTVEA DRLHPMFLAM ADARAVLIKL ADRLHNMKTL YALSPVKQQR FAKETLEIFA
PLANCLGIST WKVQLENLCF KHLYPNQHNE MSTMLEDSFD EAMITSAIEK LDQALKKAGI
SYHVLCGRHK SLYSIYSKML KKKLTVDEIH DIHGLRLIVD NEGDCYKALG VVHSLWSEVP
GKLKDYITHP KFNGYQSLHT VVMDNGTVPL EVQIRTQEMH LQAEFGFAAH WRYKEGGCKY
SSFVLQMVEW ARWVVTWHCE AMSKDRSSIS SSDSIKPPLQ VFRLTLEDCP ASYKPNSSQD
GPVYVIVIEN DKMSVQEFPA SSTVSDLLSR AGPGSSRWSM YGIPAKEELR PRLNQIPVSD
LKWKLKMGDV VELTPKIPDE SLTEYREEIQ RMYDRGLAFS RPGTMVGWGS