ID A0A0G0YUR2_9BACT Unreviewed; 479 AA.
AC A0A0G0YUR2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:KKS13411.1};
GN ORFNames=UU67_C0025G0002 {ECO:0000313|EMBL:KKS13411.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWB1_41_5.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618429 {ECO:0000313|EMBL:KKS13411.1, ECO:0000313|Proteomes:UP000034753};
RN [1] {ECO:0000313|EMBL:KKS13411.1, ECO:0000313|Proteomes:UP000034753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- 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:KKS13411.1}.
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DR EMBL; LCBN01000025; KKS13411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0YUR2; -.
DR PATRIC; fig|1618429.3.peg.560; -.
DR Proteomes; UP000034753; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 479 AA; 54136 MW; 5595B76E2CCE6541 CRC64;
MNYLEIPLVK KAYDFAETSL AGQKRLSGEE ILEHCVKVAD NLMKFDVTDP KTLSAAILHH
SILNGAATPE DLKEEFGEDI AGILNAFHKL HIVKFRKGTE KEFAEELRKM FLVLARDLRV
VLIKMCDILD NLRTLSCLTR EKGEEVARET LEIFAPLAER LGIGEMKGEM QDLAFAYLER
ASCDKTKQLL QTNLVELNII LTKIKDELKK SLGKAGIHYR IESRTKHLYS LYMKLCRPEI
NFDMSKVSDL IAFRIVVSTT EDCYKVLDIV HKLWKPVSGS VSDFITHPKP NGYRSIHTKV
VGPQGRIFEI QIRTEEMHEE AEYGLAAHWN YAEMKSRGVS DAEVSRGFAT SAEKLEWVKN
LAKWQKEVTN DSEFLKSVKT DFFGERVFCF TPGGDVKDLP AGATPVDFAY CLHTEVGDGC
SGAKVNGKMV PLDFKIQNGD VVEIILGKGN KKPNRDWLEF TVTSSAKAQI RKHFKTIKP
//
