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
//