ID A0A0D3LKC7_9BACT Unreviewed; 736 AA.
AC A0A0D3LKC7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=(P)ppGpp synthetase I SpoT/RelA {ECO:0000313|EMBL:AHM62455.1};
GN ORFNames=D770_21030 {ECO:0000313|EMBL:AHM62455.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM62455.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM62455.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM62455.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP004371; AHM62455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LKC7; -.
DR STRING; 1257021.D770_21030; -.
DR KEGG; fbt:D770_21030; -.
DR PATRIC; fig|1257021.3.peg.4744; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000064112; Chromosome.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
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; PF19296; RelA_AH_RIS; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000064112}.
FT DOMAIN 402..465
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 736 AA; 85065 MW; CFA96B295857881A CRC64;
MVTIDLEAEK QEIIRRYRKL LRHAKPFLKD GDAKIIKKAF HTSSEAHREM RRKSGEPYIY
HPLAVAQICV DEIGLGTTSI VAALLHDVVE DTELELEDIQ RDFGPKVARI IDGLTKISGV
FEHGRSQQAE NFRKMLLTLS EDVRVILIKL ADRLHNMRTL DSMPRHKQLK IASETMYLYA
PLAHRLGLYA IKSELEDLYL KYTEPATYRE IARKISTTRA ARTKFIRQFT KPIEDELRRF
GLHFVIKGRP KSIYSIWNKM RKQNIPFEEV YDLFAIRVIV DADDEQEKAA CWQVYSVVTD
FYKPNPDRLR DWISTPKANG YESLHTTVMS STGSWVEVQI RTSRMDEIAE KGYAAHWKYK
EHKSVQSKEM GLELWISRVR EMLEASNASA IEFVDDFRSN LFQEEVFVFT PKGELKTLPI
GATALDFAFD IHTEIGAHCI GAKVNQRLVP LNHALKNGDQ VEILTSEKQK PNEDWLRFVV
SSKAIARIKE CLKEDKKSAA IDGREIVERK LKQMKLQPNH EIINQLRAFF DCKTPLEFYY
KVGTGQIDPK DVKRFREFRD ERKQLKKPEI QDAQTFEQEI RKVKSSEQDY LLIGEDMNVV
DYKLSRCCSP IPGDDVFGFV TVNEGIKIHR VTCPNAVELL SNYGYRVVKA KWTSRQKIAF
LAGLKIDGTD RVGLINDITK IISDELHVNM QSVSIETEDG IFEGTIRLYV NDTRHLDLLI
KKLEKVEGIN KAFRFN
//
