ID   RELA_STRCO              Reviewed;         847 AA.
AC   P52560; P72401;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
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; OrderedLocusNames=SCO1513; ORFNames=SCL2.03c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=8825780; DOI=10.1046/j.1365-2958.1996.390919.x;
RA   Chakraburtty R., White J., Takano E., Bibb M.J.;
RT   "Cloning, characterization and disruption of a (p)ppGpp synthetase gene
RT   (relA) of Streptomyces coelicolor A3(2).";
RL   Mol. Microbiol. 19:357-368(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / J802;
RX   PubMed=8631867; DOI=10.1074/jbc.271.18.10627;
RA   Martinez-Costa O.H., Arias P., Romero N.M., Parro V., Mellado R.P.,
RA   Malpartida F.;
RT   "A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls
RT   antibiotic biosynthetic genes.";
RL   J. Biol. Chem. 271:10627-10634(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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. PppGpp could play an essential role in triggering
CC       antibiotic production under some nutritional conditions.
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   -!- INDUCTION: By amino acid starvation. Activation through the binding of
CC       uncharged tRNA in the acceptor sites of translating ribosomes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; X87267; CAA60717.1; -; Genomic_DNA.
DR   EMBL; X92520; CAA63297.1; -; Genomic_DNA.
DR   EMBL; AL939109; CAB70915.1; -; Genomic_DNA.
DR   PIR; S70687; S70687.
DR   RefSeq; NP_625792.1; NC_003888.3.
DR   RefSeq; WP_003977314.1; NZ_VNID01000021.1.
DR   AlphaFoldDB; P52560; -.
DR   SMR; P52560; -.
DR   STRING; 100226.SCO1513; -.
DR   PRIDE; P52560; -.
DR   GeneID; 1096939; -.
DR   KEGG; sco:SCO1513; -.
DR   PATRIC; fig|100226.15.peg.1522; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_11; -.
DR   InParanoid; P52560; -.
DR   OMA; DWISSPK; -.
DR   PhylomeDB; P52560; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000001973; Chromosome.
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:0015970; P:guanosine tetraphosphate biosynthetic process; IMP:CACAO.
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   ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..847
FT                   /note="GTP pyrophosphokinase"
FT                   /id="PRO_0000166564"
FT   DOMAIN          149..246
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          503..564
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          768..842
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..63
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        197
FT                   /note="V -> L (in Ref. 2; CAA63297)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   847 AA;  94182 MW;  544040B21A0D512E CRC64;
     MPDEAQPLTA AKPESASASA AKPAPSAPQA KNDTHGPIQH APAAPVDKPA EQQPRPKPLP
     AERPQNAPVV RAPAGQPARS GSSNRVRARL ARLGVQRANP YNPVLEPLLR IVRGNDPKIE
     TSTLRQIERA YQVAERWHRG QKRKSGDPYI THPLAVTTIL AELGMDPATL MAGLLHDTVE
     DTEYGLEDLR RDFGDVVTLL VDGVTKLDKV KFGEAAQAET VRKMVVAMAK DPRVLVIKLA
     DRLHNMRTMR YLKREKQEKK ARETLEIYAP LAHRLGMNTI KWELEDLAFA ILYPKMYDEI
     VRLVAERAPK RDEYLAVVTD EVQQDLRAAR IKATVTGRPK HYYSVYQKMI VRGRDFAEIY
     DLVGIRVLVD TVRDCYAALG TVHARWNPVP GRFKDYIAMP KFNMYQSLHT TVIGPGGKPV
     ELQIRTFDMH RRAEYGIAAH WKYKQEAVAG ASKVRTDAPK SSGKSKDDHL NDMAWLRQLL
     DWQKETEDPG EFLESLRFDL SRNEVFVFTP KGDVIALPAG ATPVDFAYAV HTEVGHRTIG
     ARVNGRLVPL ESTLDNGDLV EVFTSKAAGA GPSRDWLGFV KSPRARNKIR AWFSKERRDE
     AIEQGKDAIV RAMRKQNLPI QRILTGDSLV TLAHEMRYSD ISALYAAIGE GHVSAPNIVQ
     KLVQALGGEE AATEEIDESV PPSRGRGRKR RANADPGVVV KGVEDVWVKL ARCCTPVPGD
     PIIGFVTRGS GVSVHRSDCV NVDSLSREPE RILEVEWAPT QSSVFLVAIQ VEALDRSRLL
     SDVTRVLSDQ HVNILSAAVQ TSRDRVATSR FTFEMGDPKH LGHVLKAVRG VEGVYDVYRV
     TSARRPS