ID A0A264W0K8_9BACL Unreviewed; 729 AA.
AC A0A264W0K8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CF394_13205 {ECO:0000313|EMBL:OZS77093.1};
OS Tetzosporium hominis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Tetzosporium.
OX NCBI_TaxID=2020506 {ECO:0000313|EMBL:OZS77093.1, ECO:0000313|Proteomes:UP000217065};
RN [1] {ECO:0000313|EMBL:OZS77093.1, ECO:0000313|Proteomes:UP000217065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-49 {ECO:0000313|EMBL:OZS77093.1,
RC ECO:0000313|Proteomes:UP000217065};
RA Tetz G., Tetz V.;
RT "Tetzosporium hominis gen.nov. sp.nov.";
RL Submitted (JUL-2017) 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:OZS77093.1}.
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DR EMBL; NOKQ01000289; OZS77093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264W0K8; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000217065; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000217065};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
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 656..729
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 729 AA; 83292 MW; 42A97FEA00536C6D CRC64;
MAKEQVRTAE EVFAITATYM NETNVRFVEK AYKLAEHAHR NQFRNSGEPY IIHPIQVAGI
LADLQMDPET VAAGFLHDVI EDTEYTREDL VKEFSEEVAM LVEGVTKLGK IKYMSKEEQQ
AENHRKMFIA MAQDIRIILI KLADRLHNMR TLKHLPEEKQ RRIANETLEI FAPLAHRLGI
STVKWELEDT SLRYLNPQQY YRIVNFMKKK RTEREAYLNH VMKDINSQLD EVGIQADISG
RPKHIYSIYR KMVIQQKQFN EIYDLLAMRI IVDSIKDCYA VLGIIHTLWK PMPGRFKDYI
AMPKQNLYQS IHTTVIGPNG DPLEVQIRTQ EMHNIAEYGV AAHWAYKEGR KVETSDESVD
TKLSWFREIL EFQNESSNAE EFMESLKFDL FSDMVYVFTP KGDVIELPAG SVPIDFAYRV
HSEVGNKTIG AKVNGKMVPL DTKLKTGDII EVLTSKQSFG PSRDWLKIAQ SSQAKNKIKQ
FFKKQQRDEN IEKGKEAIDK EIRSQDFDPK VVLTSENLKR VCEKYAFTSE EDLYSAVGFG
GITAQQVVNR LAEKMRKERD HEETLEKISK NMASPPVKKS TESGVVVKGI DNLLIRLSRC
CSPVPGDEIV GFITKGRGVS VHRADCPNVQ GADSNQRLID VEWEQDTSAK KEYAVDIEVA
AFDRTGLLNE VLMAVTDSKT TIAAVTGKSE KDIATINLTI KITNISHLHR VVDRIKQLPN
VYSVQRIIN
//
