ID A0A0G0TZA8_9BACT Unreviewed; 501 AA.
AC A0A0G0TZA8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:KKR52535.1};
GN ORFNames=UT89_C0001G0043 {ECO:0000313|EMBL:KKR52535.1};
OS Parcubacteria group bacterium GW2011_GWE1_40_20.
OC Bacteria.
OX NCBI_TaxID=1618946 {ECO:0000313|EMBL:KKR52535.1, ECO:0000313|Proteomes:UP000034131};
RN [1] {ECO:0000313|EMBL:KKR52535.1, ECO:0000313|Proteomes:UP000034131}
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:KKR52535.1}.
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DR EMBL; LBYN01000001; KKR52535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0TZA8; -.
DR PATRIC; fig|1618946.3.peg.45; -.
DR Proteomes; UP000034131; 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; 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; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 44..142
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 406..469
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 501 AA; 57866 MW; 79BC78A385755B2F CRC64;
MNDIKEIVSL LYNPTENDIA LIQKAYDFAR KAHATHKRNS GEEYFNHLFA TAKNIAELGM
SPTTISAGFL HDMLEDTDIT SEEVEKEFGR EILFLIEGVT KLGEIKYRGT NRYNESLRKL
FVAMSQDIRV LIVKLCDRLH NMQTLAYVPE EKQLRIAKET LEIYAPIASR LGIKKLQREL
EDISFMYVYP EDWKNVQDLL KTKEKEQEKY LEKFEKLIKK ELAKNNIIDF KIDHRVKGMY
SLYKKLKQKD MDIEKVYDIS ALRITVPDIA DCYKILGIIH GSWRPLPGRI KDYIASPKLN
GYRSIHTTIF SGDGGIIEVQ IRTEDMHKEA EYGIASHLSY KEGIKKKTTN PDLLWVTKIL
PWKQNENPNA GIHSSSVDIP HWVKELVEYQ KETGDGLVDE IKDDFFEERI FVFTPIGDVI
DLPKDSSVID FAYAIHTDIG SHMSGAKVNG KFVALSTILQ NGDRVEIETK KSSKPSRKWL
EFCKTTMAKR RINNYLENNK K
//
