ID A0A0G1YVV3_9BACT Unreviewed; 571 AA.
AC A0A0G1YVV3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:KKW47315.1};
GN ORFNames=UZ00_C0009G0001 {ECO:0000313|EMBL:KKW47315.1};
OS Parcubacteria group bacterium GW2011_GWA1_60_11.
OC Bacteria.
OX NCBI_TaxID=1618805 {ECO:0000313|EMBL:KKW47315.1, ECO:0000313|Proteomes:UP000034313};
RN [1] {ECO:0000313|EMBL:KKW47315.1, ECO:0000313|Proteomes:UP000034313}
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:KKW47315.1}.
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DR EMBL; LCSF01000009; KKW47315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YVV3; -.
DR PATRIC; fig|1618805.3.peg.195; -.
DR Proteomes; UP000034313; 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; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 37..135
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 494..571
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 571 AA; 64858 MW; 023B87958A193C26 CRC64;
MNVKEFSEKN PASLVGRAYA LAKKAHAGQK RTSGEPYFAH PLAAAQHVAD WNLDEQSIAA
ALLHDVAEDT SISIEELRTE FGEDVAFLVD GVTKLGKIKY RGVETQVENL RKMILALSED
IRVVIVKLGD RLHNMTTLAA LPPQKQRRIA LETMDIYAPL AYRLGMQGLS GELEDLAFPY
IYPQEYKWLI ENVSERYEER ERYLDRVKPI AVKELAANGI TPLTVDSRAK RYSSLYKKLL
RYEMDVEKIY DLVALRIVVS SVEECYAALG IIHKLWPPLP GRIKDYIALP KPNGYRSLHT
TVFCLDQKIT EIQIRTQEMH EESENGIAAH WAYEQIKGGK AYARRQAVTA EKKELAWVQQ
LRSWQKEFTN PEEFISSLKI DFFRDRIFAI TPKGEVMDLP AGASPIDFAY QVHSAIGDTC
SGAKVNGKIV PLNYELRSGD VVEIMTQKNK LPSESWLEFV TTASAKHHIR MRLRNSGRAS
GSLAKVSRAP THVEFRLTVE DRIGLLKDIS VMLSRSHLNI VSLNTQNPEV RGKFPVLRIK
CDTADKEKIE KLVLKLKTIR EVREISYRLL I
//
