ID   A0A1F8RJD1_9CHLR        Unreviewed;       723 AA.
AC   A0A1F8RJD1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:OGO47835.1};
GN   ORFNames=A2W34_02175 {ECO:0000313|EMBL:OGO47835.1};
OS   Chloroflexi bacterium RBG_16_64_32.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797658 {ECO:0000313|EMBL:OGO47835.1, ECO:0000313|Proteomes:UP000179752};
RN   [1] {ECO:0000313|EMBL:OGO47835.1, ECO:0000313|Proteomes:UP000179752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO47835.1}.
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DR   EMBL; MGNZ01000051; OGO47835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8RJD1; -.
DR   STRING; 1797658.A2W34_02175; -.
DR   Proteomes; UP000179752; Unassembled WGS sequence.
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; IPR006674; HD_domain.
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; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
FT   DOMAIN          43..148
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          392..453
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          643..717
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   723 AA;  81098 MW;  4194AA7731262D30 CRC64;
     MAQPLLAKAR EFLPSDAVAK VQAAYEFAAN SHAGQLRRSG DPVITHPLHA ALTIAALQLD
     GDTIAAALLH DVQEDCGVTN AEIEKRFGPE VAKLVEGVTK LGQIPWEAAE AAAADDHIQA
     ENLRKMFLAM AQDLRVVIIK LADRLHNMLT LKALPPDDQI RISRETMEVY APLASRLGIW
     EMKWQLEDLA FRHLDPDRYK AIAGMLDVKR DARERQVARV KEFLSEELAK QGVKADVQGR
     AKHIYSIYQK IEKYAATSRG SSEIYDLLAV RILVNTVTDC YSALGVVHGL WRPLPGAFDD
     YIANPKESMY QALHTTVMSL DTRPLEVQIR TYEMHRSAEY GVAAHWRYKE GSKRDLRYEE
     RLAWLRQLLE WHREIAQAEE LVEAVKSDIF QDQVFVFTPK GAVKDLPKGG TPIDFAYRIH
     TDLGHMCVGA KVNGRLVTLN TELNNGDVVE VMTGKSSKGP SRDWLNAHLG YVHTSHARGK
     IRQWFKRQER DENIARGHEM LEKELHRLGV TMADVQQDLL KLFHCDDLED FLQRTGYGEI
     STHQIAKRLA PIIQPEEIAV PPPEAPARAT YTTSVSVLGT GDLLTRLARC CNPVPGDDII
     GYVTRGEGVS IHRGDCPNIL HAGERERLVE VEWGQRGHLY PVAVRIEAWD RVGLLRDVST
     MVALERVNMV GVHTQEQEDG LITIFVTLET TGIEQLTRLL SKLEGVRGVL SVGRRLESTT
     KKG
//