ID   B3EFX2_CHLL2            Unreviewed;       733 AA.
AC   B3EFX2;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACD89505.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:ACD89505.1};
GN   OrderedLocusNames=Clim_0412 {ECO:0000313|EMBL:ACD89505.1};
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD89505.1, ECO:0000313|Proteomes:UP000008841};
RN   [1] {ECO:0000313|EMBL:ACD89505.1, ECO:0000313|Proteomes:UP000008841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330
RC   {ECO:0000313|Proteomes:UP000008841};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) 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; CP001097; ACD89505.1; -; Genomic_DNA.
DR   RefSeq; WP_012465386.1; NC_010803.1.
DR   AlphaFoldDB; B3EFX2; -.
DR   STRING; 290315.Clim_0412; -.
DR   KEGG; cli:Clim_0412; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_10; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000008841; Chromosome.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; PS51671; ACT; 1.
DR   PROSITE; PS50889; S4; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW   Transferase {ECO:0000313|EMBL:ACD89505.1}.
FT   DOMAIN          394..455
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          660..733
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          548..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  83646 MW;  2A838ACAC1537082 CRC64;
     MLAQIDKKHY EKLHEILRLC RSNLKHSDES LIQRAFFMCY RAHDGEKRAS GEPYFYHPVE
     VATILLEELP LDDVSVAAAL LHDVIEDSGY TYEDLVAELG VEVADIVEGL TKISGIMINR
     EITQAEGFRK MLLSMVKDIR VILIKFCDRL HNMRTLESLP EHRRLKIALE TRDIYAPLAH
     RFGLGKMKVE FENLALKYID PEMYEFLQQK IKLSRAERIN YLNKMISPIK DDLEKQGFRI
     EVEGRAKHLF SIYNKMRNKN KTFEDIHDLY GIRVIVDTER VAECFAVYGF ITQKYPPIPQ
     HFKDYISIPK HNGYQSLHSA IIGPKGYVVE LQIRTTRMHE FAELGVAAHW RYKEKISKDD
     ASIDSFLRWA RELIKDADSA ASFMEGFKLN LYHDEIYVFT PKGDMKTMPA SATPIDFAYA
     IHSEIGNGCI GAKVNGKIVR LNAQLKSGDR VEIITSKNQK PKSDWLKFVV THRARLKIRS
     AINEERRLQI EKGRSMWEKL LSGGKKLFSD NDIIRQAKKY GIRTPADFFS ALASQQISGE
     EIFERVSNAR KEPPEAGAKA SSSEAKQVED YLQQARQDQD APVSKKDDVV IAGMTNIAYA
     YAKCCQPVPG DDVIGFVTAE GLVKIHRKNC LNVSNENLLK SERIVSVAWN RKVETDFLAG
     IKIVGEDRIG ITNQITAVIS KFDTNIRSIS LHARDGMFVG TLMVYVRNIE KLGTLMEKLK
     KVQGIFTVER LIS
//