ID   D4IPR9_9BACT            Unreviewed;       739 AA.
AC   D4IPR9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:CBK64931.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:CBK64931.1};
GN   ORFNames=AL1_27930 {ECO:0000313|EMBL:CBK64931.1};
OS   Alistipes shahii WAL 8301.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK64931.1, ECO:0000313|Proteomes:UP000008794};
RN   [1] {ECO:0000313|EMBL:CBK64931.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64931.1,
RC   ECO:0000313|Proteomes:UP000008794};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J.;
RT   "The genome sequence of Alistipes shahii WAL 8301.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK64931.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64931.1,
RC   ECO:0000313|Proteomes:UP000008794};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929032; CBK64931.1; -; Genomic_DNA.
DR   RefSeq; WP_015547736.1; NZ_CP102253.1.
DR   AlphaFoldDB; D4IPR9; -.
DR   STRING; 717959.AL1_27930; -.
DR   GeneID; 66248994; -.
DR   KEGG; ash:AL1_27930; -.
DR   PATRIC; fig|717959.3.peg.1293; -.
DR   HOGENOM; CLU_012300_3_0_10; -.
DR   OrthoDB; 9805041at2; -.
DR   BioCyc; ASHA717959:AL1_RS13145-MONOMER; -.
DR   Proteomes; UP000008794; Chromosome.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008794};
KW   Transferase {ECO:0000313|EMBL:CBK64931.1}.
FT   DOMAIN          403..464
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   739 AA;  84221 MW;  4EC3854C3A771408 CRC64;
     MGYTAEDENL IKEKWDDLLL SCTKICKNDE DWNFIKRAFF LAKEAHEGVR RRSGEPYLLH
     PIAVAKIVIE EIGLGVKSVV AALLHDVVED TEYSVEDMER IFGPKIASMV DGLTKMSGVF
     NADTSEQAEY FRKVLLTLSD DVRVILIKIA DRLHNMRTLG AMPMNKQIKI TGETIYLFAP
     LAYRLGLYSI KSELEDLCMK YRFPQQYAEI TQKLQESEAS RREFINKFNA PIIASLNRDN
     INYEISGRVK SVYSIWSKMQ RKQIPFEEIY DLFAIRIVFK PLPFPSEKTQ CWQIYSTITD
     IYTPKPDRLR DWISMPKANG YEALHSTVMG PDGVWVEVQI RTQRMEDIAE RGFAAHWKYK
     HATISQDEDE FDKWLKQIRA ALNSPTENAV DFLDNFKLSL YTSEIVVFTP KGEARKMPFG
     ATALDFAYDI HSKIGNSAIS AKINHKLEPI TTQINSGDQI EIITADNARP KPEWLETVTT
     AKAKQSIKSF LKRERQNNIE RGMQMLDEKM KSLNVKLSGR VLRKITPIYD SKNKEELYSK
     IGAGIVSLDN LDKALKVNSK SKILKFWTLF IPQKKEDETD DAAIPGEIAP AEEAPATEPQ
     FEIAECCKPI PGDKVVGYRD PASGNIIVHK ATCDELNRLA TQFGRNIVKE EIKWSQHKAM
     SYLVTTELRG IDRQGILLDL AKVVSADFNI NIREVNIHSH DGIFEGNVSL YVKDAESLHA
     VMDKLRKIKG IESVKRTLS
//