ID A0A150F3J5_9BACI Unreviewed; 734 AA.
AC A0A150F3J5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AXI58_03025 {ECO:0000313|EMBL:KXZ15248.1};
OS Bacillus nakamurai.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1793963 {ECO:0000313|EMBL:KXZ15248.1, ECO:0000313|Proteomes:UP000075430};
RN [1] {ECO:0000313|EMBL:KXZ15248.1, ECO:0000313|Proteomes:UP000075430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41092 {ECO:0000313|EMBL:KXZ15248.1,
RC ECO:0000313|Proteomes:UP000075430};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:KXZ15248.1}.
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DR EMBL; LSBA01000036; KXZ15248.1; -; Genomic_DNA.
DR RefSeq; WP_061522908.1; NZ_LSBA01000036.1.
DR AlphaFoldDB; A0A150F3J5; -.
DR STRING; 1793963.AXI58_03025; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000075430; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 392..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..734
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 543..570
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 734 AA; 84874 MW; FEBC5E27764FACD9 CRC64;
MANEQVLTAE QVIDKARTYL PEEQIAFVEK AYLYAQDAHR EQYRKSGEPY IIHPIQVAGI
LVDLEMDPST IASGFLHDVV EDTDVTLDDL KEAFSEEVAM LVDGVTKLGK IKYKSQEEQQ
AENHRKMFVA MAQDIRVILI KLADRLHNMR TLKHLPQEKQ RRISNETLEI FAPLAHRLGI
SKIKWELEDT ALRYLNPQQY YRIVNLMKKK RAERELYVDE VVNEVKKRVE EVNIKADFSG
RPKHIYSIYR KMALQNKQFN EIYDLLAVRI LVGSIKDCYA VLGIIHTCWK PMPGRFKDYI
AMPKPNMYQS LHTTVIGPKG DPLEVQIRTF EMHEIAEYGV AAHWAYKEGK AANEEATFEK
KLSWFREILE FQNESTDAEE FMESLKIDLF SDMVYVFTPK GDVIELPSGS VPIDFSYRIH
SEIGNKTIGA KVNGKMVTLD HKLRTGDIVE ILTSKHSYGP SQDWVKLAQT SQAKHKIRQF
FKKQRREENV EKGRELVEKE IKNLDFEVKD VLTPDNLQKV ADKFNFTNEE DMYAAVGYNG
ITALQVANRL TEKERKLRDQ EEQEKIVQEV TAEPKQYPQG RKREAGVRVK GIDNLLVRLS
KCCNPVPGDH IVGFITKGRG VSVHRDDCPN VKTNEAQERL IPVEWEHESH VQKRKEYNVE
IEILGYDRRG LLNEVLQAVN ETKTNISSVS GKSDRNKVAT IHMAIFIQNI NHLHKVVERI
KQIKDIYSVR RVMN
//
