ID   RELA_STRAT              Reviewed;         841 AA.
AC   O85709;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=GTP pyrophosphokinase;
DE            EC=2.7.6.5;
DE   AltName: Full=(p)ppGpp synthase;
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
DE   AltName: Full=ppGpp synthase I;
GN   Name=relA;
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 41481 / IMRU 3720;
RX   PubMed=10368159; DOI=10.1128/jb.181.12.3824-3829.1999;
RA   Hoyt S., Jones G.H.;
RT   "relA is required for actinomycin production in Streptomyces
RT   antibioticus.";
RL   J. Bacteriol. 181:3824-3829(1999).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       This enzyme catalyzes the formation of pppGpp which is then hydrolyzed
CC       to form ppGpp (By similarity). Is required for actinomycin production.
CC       {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   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       1/2.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AF072829; AAC26021.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85709; -.
DR   SMR; O85709; -.
DR   STRING; 1890.AFM16_07730; -.
DR   UniPathway; UPA00908; UER00884.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR002912; ACT_dom.
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; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF19296; DUF5913; 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; SSF55021; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; GTP-binding; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..841
FT                   /note="GTP pyrophosphokinase"
FT                   /id="PRO_0000166563"
FT   DOMAIN          146..243
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          499..560
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          763..837
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  93672 MW;  632A037BA4EF4C94 CRC64;
     MPDEAQHLTA AKPDSAAGAA AEPAAHAQDG GGPVEHDRSA PADKPAERTR PKPAPPERPR
     PPPPRARAAG QPAARSGGSS NRVRARLARL GVQRANLTHP VLEPLLRIVR ANDPKIETST
     LRQIEKAYQV AERWHRGQKR KSGDPYITHP LAVTTILAEL GMDPATLMAG LLHDSREDTE
     YGLDDLRRDF GDVVGLLVDG VTKLDKVKFG EAAQAETVRK MVVAMAKDPR VLVIKLADRL
     HNMRTMRYLK REKQEKKARE TLEIYAPLAH RLGMNTIKWE LEDLAFAILY PKMYDEIVRL
     VAERAPKRDE YLAIVTDEVQ SDLRARRIKA TVTGRPKHYY SVYQKIIVRG RDFAEIYDLV
     GIRVLVDTVR DCYAALGTVH ARWNPVPGRF KDYIAMPKFN MYQSLHTTVI GPNGKPVELQ
     IRTFDMHRRA EYGIAAHWKY KQEAVARASK VRTDVPKPAK GKDDHLNDMA WLRQLLDWQK
     ETEDPGEFLE SLRFDLSRNE VFVFTPKSDV IALPAGATPV DFAYAVHTEV GHRTIGARVN
     GRLVPLESTL DNGDLVEVFT SKAAGAGPSR DWLGFVKSPR ARNKIRAWFS KERRDEAIEQ
     GKDAIARAMR KQNLPIQRIL TGDSLVTLAH EMRYPDISSS DAAIGEGHVG AQNVVQKLVQ
     ALGGEEAASE EIDEAVPSRS RSRKRRSNQD PGVVVKGVDD VWVKLARCCT PVPGEPIIGF
     VTRGSAVSVH RSDCVNVESL AREPERILEV EWAPTQSSVF LVAIQVEALD RSRLLSDVTR
     VLSDQHVNIL SAAVQTSRDR VATSRFTFEM GDPKHLGHVL KAVRGVEGVY DVYRVTPGPQ
     P