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Database: UniProt
Entry: A0A0G0NHQ9_9BACT
LinkDB: A0A0G0NHQ9_9BACT
Original site: A0A0G0NHQ9_9BACT 
ID   A0A0G0NHQ9_9BACT        Unreviewed;       503 AA.
AC   A0A0G0NHQ9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:KKQ85444.1};
GN   ORFNames=UT08_C0006G0027 {ECO:0000313|EMBL:KKQ85444.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWB1_38_8.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618570 {ECO:0000313|EMBL:KKQ85444.1, ECO:0000313|Proteomes:UP000034081};
RN   [1] {ECO:0000313|EMBL:KKQ85444.1, ECO:0000313|Proteomes:UP000034081}
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   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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:KKQ85444.1}.
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DR   EMBL; LBVL01000006; KKQ85444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0NHQ9; -.
DR   STRING; 1618570.UT08_C0006G0027; -.
DR   PATRIC; fig|1618570.3.peg.681; -.
DR   Proteomes; UP000034081; Unassembled WGS sequence.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; IPR006674; HD_domain.
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; GTP PYROPHOSPHOKINASE; 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; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
FT   DOMAIN          50..150
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          403..467
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   503 AA;  58074 MW;  C675C83E70C19248 CRC64;
     MEKKLEGRFE QLVKTIHEYN ENVDLVRIRR AFEFAKLAHA GEKRISGSEV IWHPLETSII
     LASWKMDIAT IVAGLLHDTI EHGAATEKDI SEYFGEEVLG LVKGVTKVSK IKLKGSSDEI
     FVENLRKMFL AIAKDLRIVF LRLAERIDNL KSYEYVPEEQ RKLYAKDSLE IYAPLAERLG
     MWEVKTQIDD LSFPYVYPQE YQKVKKLSAL YYKDAEKRVE KMKKNLLRQL KREGVDAKIH
     GRKKGLFSLW KKLDRPEIDW DLAKIHDIVA LRMLVEEVSE CYVALGIVHK YFKPIPHIAL
     ADFIAVPKPN GYSSIHTKVF GENDKAVEIQ ITTHNLHEEN QYGLAAHWHL SLIKSRKGIS
     SKDIDVGKHN VVGKKFEWVE KLAEWQKEIS DSEEFLKAVK FDALSRRIFV FSPKGDVFDL
     PMNATPVDFT FAVHSDLGDY IKAAKVDGKI VPLNYKLKSG QVVEILKSKE KRLPSHDWLE
     FVVTNFARRE ITKTIRKNDV DRN
//
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