ID   RELA_PHOAS              Reviewed;         744 AA.
AC   P55133;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 114.
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   Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS   CCUG 15956)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=7928955; DOI=10.1128/jb.176.19.5949-5957.1994;
RA   Flaerdh K., Axberg T., Albertson N.H., Kjelleberg S.;
RT   "Stringent control during carbon starvation of marine Vibrio sp. strain
RT   S14: molecular cloning, nucleotide sequence, and deletion of the relA
RT   gene.";
RL   J. Bacteriol. 176:5949-5957(1994).
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. Also plays a role in the reductive division that occurs
CC       during the initial phase of nutrient starvation.
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   -!- DISRUPTION PHENOTYPE: Mutants remain rod shaped, and do not acquire the
CC       typical coccoid morphology usually seen during starvation.
CC       {ECO:0000269|PubMed:7928955}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; U13769; AAA62208.1; -; Genomic_DNA.
DR   RefSeq; WP_005371455.1; NZ_CH902602.1.
DR   AlphaFoldDB; P55133; -.
DR   SMR; P55133; -.
DR   GeneID; 61230661; -.
DR   eggNOG; COG0317; Bacteria.
DR   OrthoDB; 9805041at2; -.
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:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04876; ACT_RelA-SpoT; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 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; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
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   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF40; GTP PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF19296; RelA_AH_RIS; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 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; 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; Transferase.
FT   CHAIN           1..744
FT                   /note="GTP pyrophosphokinase"
FT                   /id="PRO_0000166566"
FT   DOMAIN          54..159
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          403..464
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          669..744
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   744 AA;  84546 MW;  B7AC772C4D47A40C CRC64;
     MVAVRGAHLK ENTTFELVSW VESLRQDAKV SSRIEGTYQR CIELAAEQEN GPLLLWRGRE
     LVEILVTLSM DADTLIAALL YPLVEGGCYS TDALKEEYSG TILHLVQGVE QMCAISQLKS
     TAEETAQAAQ VDNIRRMLLS MVDDFRCVVI KLAERICNLR EVKDQPDEVR RAAAQECANI
     YAPLANRLGI GQLKWEIEDY AFRYQHPDTY KQIAKQLSER RIDREDYITH FVDDLSDAMK
     ASNIRAEVQG RPKHIYSIWR KMQKKSLEFD ELFDVRAVRI VAEELQDCYA ALGVVHTKYR
     HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV AAHWKYKEGT
     ASGGAQSAYD EKINWLRKLL AWQEEMSDSG EMLDELRSQV FDDRVYAFTP KGDVVDLPSN
     ATPLDFAYHI HSEVGHRCIG AKVEGRIVPF TYHLQMGDQV EIITQKEPNP SRDWLNPNLG
     FVTSSRARAK VHAWFRKQDR DKNIIAGKEI LEAELVKIHA TLKDAQYYAA KRFNVKSPEE
     LYAGIGSGDL RINQVINHIN ALVNKPTAEE EDQQLLEKLS EASNKQATSH KKPQRDAVVV
     EGVDNLMTHL ARCCQPIPGD DIQGFVTQGR GISVHRMDCE QLEELRHHAP ERIIDTVWGG
     GFVGNYTITV RVTASERNGL LKELTNTLMN EKVKVAGMKS RVDYKKQMSI MDFELELTDL
     EVLGRVLKRI EQVKDVAEAK RLYG
//