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Database: UniProt
Entry: A0A0L0QPX2_VIRPA
LinkDB: A0A0L0QPX2_VIRPA
Original site: A0A0L0QPX2_VIRPA 
ID   A0A0L0QPX2_VIRPA        Unreviewed;       733 AA.
AC   A0A0L0QPX2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=AFK71_19790 {ECO:0000313|EMBL:KNE20596.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE20596.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10053 dsm26.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNE20596.1}.
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DR   EMBL; LGTO01000007; KNE20596.1; -; Genomic_DNA.
DR   RefSeq; WP_050353172.1; NZ_LGTO01000007.1.
DR   AlphaFoldDB; A0A0L0QPX2; -.
DR   GeneID; 66870209; -.
DR   PATRIC; fig|1473.5.peg.2703; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000036780; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036780}.
FT   DOMAIN          50..149
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          393..454
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          659..733
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   COILED          548..582
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   733 AA;  84659 MW;  978E7D9D513F148C CRC64;
     MAKTDIMTID DILNKAGQYL SEEDTAFIRQ AYEFAEEAHA EQFRKSGEPY IIHPVQVAGI
     LTELGMDAET IAGGFLHDVV EDTNVSVEDV EEAFNHEVAM LVDGVTKLGK IKYKSKEAQQ
     AENHRKMFVA MAKDIRVILI KLADRLHNMR TLKHLPPEKQ RRIANETLEI FSPLAHRLGI
     STIKWELEDT ALRYLNPQQY YRIVQLMKQK REQRESYIRE VMEQVSKQLR EMNIEAELSG
     RPKHLYSIYR KMVKQNKQFN EIYDLLAVRI LVNSIKDCYA VLGIIHTCWK PMPGRFKDYI
     AMPKPNLYQS LHTTVIGPKG DPLEVQIRTR EMHEIAEYGI AAHWAYKEGK QVNMDKQSFE
     EKLTWFREIL EWQNDTHDAE EFMESLKVDL FSDMVYVFTP KGDVIELPAG SVPLDFAYKI
     HTEIGNKTIG AKVNGKMEPL DYKLKNGDIV EVMTSKHSYG PSQDWLKITQ TSQAKSKIKQ
     FFKKQRREEN VLKGKEAVDR EIRSLNIEPK DVLTQEDLQR VYEKYNFSSA DDMYAAVGYQ
     GITAAAIATK LTEKLRQSRE KQQALEQTIE EVKTDVKQKK VNKRDSGVKV EGIDNLLVRL
     SKCCNPVPGD QIVGYITKGR GVSVHRSDCP NVQTEEAKQR FLHVEWENNR TEQKQYHVDL
     EISGFDRRGL VNEVLQAVNE TKTNITYVNG RSDRNKMAII QITILIHNTG HLRKIVERIK
     QIPDVYAVKR TLQ
//
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