ID A0A2V3VXC8_9BACI Unreviewed; 735 AA.
AC A0A2V3VXC8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DFR56_107113 {ECO:0000313|EMBL:PXW86592.1};
OS Pseudogracilibacillus auburnensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Pseudogracilibacillus.
OX NCBI_TaxID=1494959 {ECO:0000313|EMBL:PXW86592.1, ECO:0000313|Proteomes:UP000247978};
RN [1] {ECO:0000313|EMBL:PXW86592.1, ECO:0000313|Proteomes:UP000247978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28556 {ECO:0000313|EMBL:PXW86592.1,
RC ECO:0000313|Proteomes:UP000247978};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PXW86592.1}.
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DR EMBL; QJJQ01000007; PXW86592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3VXC8; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000247978; 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: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; 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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PXW86592.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000247978};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PXW86592.1}.
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 661..735
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 548..582
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 735 AA; 84476 MW; 0F7385C2F2AAC384 CRC64;
MSKDKNITID DIVTNAKSYL SEEDVGFIFR AYEFAKKAHE GQYRKSGEPY IVHPVQVAGI
LVDLEMDPET IAGGFLHDVV EDTDTGLEEI EAAFNSEVAM LVDGVTKLGK IKYKSKEAQQ
AENHRKMFVA MAKDIRVILI KLADRLHNMR TLKHLPSDKQ RRIANETLEI FAPLAHRLGM
STIKWELEDT ALRYLNPQQY YRIVQLMKQK RDQRESYIDD VMNAIANELA SMRIEAEISG
RPKHIYSTYR KMKTQNVQFN EIYDLLAVRV IVNSIKDCYA VLGIIHTYWK PMPGRFKDYI
AMPKANLYQS LHTTVIGPQG EPLEVQIRTK DMHKIAEYGI AAHWAYKEGK QIKTNRTSFA
EKLTWFREIL DWQNETHDAE EFVESLKIDL FSDMVYVFTP KGDVIELPSG SIPLDFAYRI
HTEIGNKTVG ARINGKMEPL DYQLKNGDIV EIITSRHSYG PSQDWLKLTQ SSQAKNKIKQ
FFKKQRKEEN IDKGKEEIEK GIKELGFTPK EVLTSENIKK ICKKFNFVNE EDLYAAVGYQ
GITASLIVTR LTDQLRKEKE SEQNLEQKIE EVQSNVQEKS GTTDKRDSGI AVEGVDNVLV
RLSRCCNPVP NDEIVGYITK GRGVSVHRKD CPNIQTDEAR ERFLEVKWKN AKYSTKEYYL
DLEISGYDRH GLLNEVLQVV NETNTQIASV SGKADKNKIA HIHLTVLIKN TDHLRHVVHR
IKQVKDIYAV TRTIQ
//
