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Database: UniProt
Entry: A4IRA0_GEOTN
LinkDB: A4IRA0_GEOTN
Original site: A4IRA0_GEOTN 
ID   A4IRA0_GEOTN            Unreviewed;       732 AA.
AC   A4IRA0;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE   AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN   OrderedLocusNames=GTNG_2509 {ECO:0000313|EMBL:ABO67854.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO67854.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO67854.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO67854.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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       {ECO:0000256|RuleBase:RU003847}.
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         Evidence={ECO:0000256|ARBA:ARBA00001157};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP000557; ABO67854.1; -; Genomic_DNA.
DR   RefSeq; WP_011887887.1; NC_009328.1.
DR   AlphaFoldDB; A4IRA0; -.
DR   KEGG; gtn:GTNG_2509; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_9; -.
DR   OMA; DWISSPK; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04876; ACT_RelA-SpoT; 1.
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; 3.30.70.260; -; 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; 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   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; 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; SM00471; HDc; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000313|EMBL:ABO67854.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}.
FT   DOMAIN          50..149
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          391..452
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          656..731
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   732 AA;  84261 MW;  52CED5E1E3837D79 CRC64;
     MANEQVLTAE QVFEQAGCYL SEQDVAFLKK AYEFAKHAHR DQFRKSGEPY IIHPIQVAGI
     LADLKMDATT IAAGFLHDVV EDTEATKEDL EREFGADVAM LVDGVTKLGK IKYKSQEEQQ
     AENHRKMFLA MAQDIRVILI KLADRLHNMR TLKHLPAEKQ RRIANETLEI FAPLAHRLGI
     SKIKWELEDT ALRYLNPQQY YRIVNLMKKK RAEREQYLEE VIQEVRERLN EVHIPCEISG
     RPKHIYSIYR KMVMQNKQFN EIYDLLAVRI IVNSIKDCYA VLGIIHTCWK PMPGRFKDYI
     AMPKPNMYQS LHTTVIGPKG EPLEVQIRTF EMHQIAEFGI AAHWAYKEGK TVKPNSFEEK
     LSWFREILEW QNDASNAEEF MESLKMDLFS DMVFVFTPKG DVIELPAGSV PIDFAYRIHS
     EIGNKTIGAK VNGKMVPLDY KLQTGDIVEI LTSKHSYGPS QDWLKLAKTS QARNKIRQFF
     KKQRREENID KGKEMVEKEV RGLGFEPKEV MTADNIKRVA EKFNFSNEDD MYAAVGYHGI
     TAAQIAHRLT EKWRKQRDLE EQQRKLAEAV SEAKLPAGKK RDCGIRVQGI DNLLIRLSRC
     CNPVPGDEII GFITRGRGIS VHRADCPNVQ VEEAADRLIP VEWESGTNGE REYNVDIEII
     GFDRRGLLNE VLQAVNETRT DISAVSGRSD HRHKIATIHM TIAIHNISHL QKVVERIKQI
     PDIYSVQRLM NN
//
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