ID   RELA_MYXXA              Reviewed;         757 AA.
AC   O52177;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 107.
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   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DK101;
RX   PubMed=9531539; DOI=10.1101/gad.12.7.1022;
RA   Harris B.Z., Kaiser D., Singer M.H.;
RT   "The guanosine nucleotide (p)ppGpp initiates development and A-factor
RT   production in Myxococcus xanthus.";
RL   Genes Dev. 12:1022-1035(1998).
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). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF025847; AAB97677.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52177; -.
DR   SMR; O52177; -.
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; 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; Transferase.
FT   CHAIN           1..757
FT                   /note="GTP pyrophosphokinase"
FT                   /id="PRO_0000166553"
FT   DOMAIN          63..165
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          406..467
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          685..757
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          13..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  84978 MW;  D6CC1000A5F72A7B CRC64;
     MWGNVAPPLV QSYDCSSFDD SPERHPPTVS QYHPDPDLDI IKKAYVYSAK VHQGQLRKSG
     EPYLVHPLEV AGILGELKLD EASIVTGLLH DTIEDTLATE EELTELFGSE VAHLVDGVTK
     LSKFSASASL SQEEKQAENF RKMIIAMAQD IRVILVKLAD RTHNMRTLDH MSEEKQARIA
     QETLDIYAPL ANRLGISWIK TELEDLSFRY VKPQEFFALQ AKLNKRKKER EKYIEDTCDL
     IRSKLAERGL KGEVSGRFKH VYSIYKKIKS QGIDFDQIHD IIAFRIIAPT APSCYEALGL
     VHEMWKPVPG RFKDFIAIPK PNMYQSLHTT IIGPLSERVE VQIRTSEMHK IAEEGIAAHW
     KYKEGKAVIS KDDEKFAWLR QLMEWQQDLK DPKEFLETVK VDLFTDEVFV FTPKGDVRSL
     PRGATPVDFA YAIHSDVGNR CVGAKVNGKI VPLRYKMKNG DTVEVLTSPQ QHPSKDWLTF
     VKTSRAQQRI RGFIKQQQRE KSLQLGRELA DRELKRFQLN FNRLLKSGEM KKAAVDLGFR
     VEDDMLVAIG YGKVTPQQLS HRLVPQEKLN AAEAGGRADA NPAATTSGGA GNSVLPGLSR
     VTDLAKRLVG RSNRSGVQIG GVDDVLVRFG RCCNPVPGDP IAGFITRGRG VTVHTVGCEK
     ALATDPERRV DVSWDVRGDF KRPVTLRVLT ADRPGLLADI TNTFSKKGVN ISQANCRATG
     DDRAVNTFEV IISDLKQLTD LMRTIERLQG VYSVERI