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
//