ID A0A0G0Z6H7_9BACT Unreviewed; 493 AA.
AC A0A0G0Z6H7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:KKS44307.1};
GN ORFNames=UV08_C0022G0004 {ECO:0000313|EMBL:KKS44307.1};
OS Parcubacteria group bacterium GW2011_GWA2_42_18.
OC Bacteria.
OX NCBI_TaxID=1618821 {ECO:0000313|EMBL:KKS44307.1, ECO:0000313|Proteomes:UP000034342};
RN [1] {ECO:0000313|EMBL:KKS44307.1, ECO:0000313|Proteomes:UP000034342}
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:KKS44307.1}.
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DR EMBL; LCDC01000022; KKS44307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0Z6H7; -.
DR STRING; 1618821.UV08_C0022G0004; -.
DR PATRIC; fig|1618821.3.peg.469; -.
DR Proteomes; UP000034342; 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 389..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 493 AA; 57066 MW; CC3BA83F2620639A CRC64;
MENTPKVEDI LKLMKRAKKN DRALVARAFE FAQKAHQGQT RVSGNPYFIH VFETARKLAE
LNMNAQTIAA GLLHDTLEDA GVPRVAMIKE FGEDITRLVD GVTKLGTVKY RGRERHIESL
RKFLMSIAED VRVLIIKLCD RLHNLRTLQY LSPEKQKRIA VESIEIYAAL ANRLGMGNLK
GDIEDAAFPY AYPKEYEMAE KLIQEKTEIN KKYLDEIYKT IKKEIIKQGI KIVKIDYRFK
HKYSLYKKLV RHNMDIDKIY DIVALRVIVP SIECCYRVLG LIHTLWRPLQ GRIKDYIAVA
KPNGYRALHT TIFTGTGGIV EIQIYTPEMY REAKYGIASH VIFKEGGFHP TSGKVRPKFA
WLNKLKDLQQ AVLEQSKFLE HLKIDFFKDR IFVFTPKGEV VDLPEESCPI DFAYTIHSDI
GDHIWSAKVN GKVIALDYKL RNGDFVEIVT KKESHPSSRW MEYVKTPLAR KHIKNYLDKN
SLMSRLSKYM PKK
//
