ID   A0A1G2DRQ4_9BACT        Unreviewed;       490 AA.
AC   A0A1G2DRQ4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=TGS domain-containing protein {ECO:0000259|PROSITE:PS51880};
GN   ORFNames=A2494_04375 {ECO:0000313|EMBL:OGZ16325.1};
OS   Candidatus Lloydbacteria bacterium RIFOXYC12_FULL_46_25.
OC   Bacteria; Candidatus Lloydbacteria.
OX   NCBI_TaxID=1798670 {ECO:0000313|EMBL:OGZ16325.1, ECO:0000313|Proteomes:UP000178106};
RN   [1] {ECO:0000313|EMBL:OGZ16325.1, ECO:0000313|Proteomes:UP000178106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ16325.1}.
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DR   EMBL; MHLU01000177; OGZ16325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2DRQ4; -.
DR   Proteomes; UP000178106; 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; SM00471; HDc; 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          390..451
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   490 AA;  55997 MW;  47204669B0827C75 CRC64;
     MERVKTLEEI TSVMRNKEQR SIALVSKAYN FSEQAHHGQK RYSGDPYFLH VSCVGYTLAE
     MGMDANTIAA GLLHDTVEDA HVSEDDIERE FGKEIRFLVD GVTKLGKLKY RGAERHVESL
     RKLFVATAKD LRVIIIKLAD RLHNVSTLKH VPKEKQKRIA METLEIYAPI ANRLSIGKIK
     GELEDYAFAF AYPEEYKKVQ DLIKERSKEN DKRLEKVYRA IQVELAKNGI TKVHGEYRIK
     RTYSLYKKLL RHNMDISDIY DLSAIRVMVP TIADCYRALG IIHSVWRPLP GRIKDYIAFP
     KPNGYQSLHT TIFTGDGGIV EIQLRTNEMN QDAAFGIAAH FAYKEKTDPK KAKGGTPRKL
     DWVGQISQLQ HSLDENSDYL ENLKADFFED RVFVFTPRGD VVDLPRDSSP IDFAFAIHSD
     IGEHTSGANV NGKFVSLDTK LKNGDIVEII TKKSSKPSKK WLEYARTTLA KKHIRSVLHE
     EDERNQQSTR
//