ID A0A0G1KGQ2_9BACT Unreviewed; 580 AA.
AC A0A0G1KGQ2;
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 I (GTP pyrophosphokinase), SpoT/RelA {ECO:0000313|EMBL:KKT82698.1};
GN ORFNames=UW79_C0002G0015 {ECO:0000313|EMBL:KKT82698.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWA2_44_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619025 {ECO:0000313|EMBL:KKT82698.1, ECO:0000313|Proteomes:UP000034032};
RN [1] {ECO:0000313|EMBL:KKT82698.1, ECO:0000313|Proteomes:UP000034032}
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:KKT82698.1}.
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DR EMBL; LCJR01000002; KKT82698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KGQ2; -.
DR PATRIC; fig|1619025.3.peg.76; -.
DR Proteomes; UP000034032; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
KW Kinase {ECO:0000313|EMBL:KKT82698.1};
KW Transferase {ECO:0000313|EMBL:KKT82698.1}.
FT DOMAIN 44..152
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 395..456
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 580 AA; 66023 MW; 2A23BCA71C2B319E CRC64;
MTELLQQIIS NPAYNDEGKA LIGKAFDFAE TAHRGQKRLS GEDYINHPLH AAYFLSELGL
DAVTVAGALL HDTVEDTPLN SKLIQEQFGK EVAFLVDGVT KLGKIEYASR DGLNKKDMDY
ARHLSSLKKM FFAMAEDIRV ILIKLADRYH NMETLRYQNK QDQQRIALET LEIYAPIAGR
LGMGRLKGQL EDLAFPYVYP DEYSKFVKMV KDKYADTNKY IERTKPVIKK HLTDAGIEVL
DMHSRSKHYF SLYQKLKNRN LELDKVFDLV AMRVIVPDIK SCYEALGVIH KYYKPFPGLI
KDYIALPKPN GYQSLHTTIF CEKGRVVEIQ IRTEDMHDHA ENGIAAHWAY SEGGKKKVTI
ADKYEIQWIS QLKKFLKETK LGESFTNLKI DFFKNRIFAF TPKGDVKDLP EGATPIDFAY
AIHSDLGHSV TGAKVNGKMV PLEFGLKNGD VVEIIKGKNK KPSFDWLEFV KTTEAKRRIK
SWFRENEVKN KSAEKDLPTR NKVKKKADYV EKVSIPGIPV IQGQRGLLYK IAKCCRPEVG
SKIKGYMTIN RGVSIHLATC KNIKDVAGKR IMSAGWAIKK
//
