ID   B3EMK0_CHLPB            Unreviewed;       731 AA.
AC   B3EMK0;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACE04939.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:ACE04939.1};
GN   OrderedLocusNames=Cphamn1_2029 {ECO:0000313|EMBL:ACE04939.1};
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE04939.1};
RN   [1] {ECO:0000313|EMBL:ACE04939.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1 {ECO:0000313|EMBL:ACE04939.1};
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., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-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; CP001101; ACE04939.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3EMK0; -.
DR   STRING; 331678.Cphamn1_2029; -.
DR   KEGG; cpb:Cphamn1_2029; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_10; -.
DR   OrthoDB; 9805041at2; -.
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:ACE04939.1}.
FT   DOMAIN          394..455
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          658..731
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   731 AA;  83682 MW;  8CAF81C3E6660D08 CRC64;
     MLAQIEKEQY EKMHEILRLA RQNLRDFDES LIQRAFFLCY RAHEGEKRAS GEPFFYHPVE
     VAKIMLTELP LDGVSVAAAL LHDVIEDSEY TYEDLTAELG SEVSDIVEGL TKISGIMINR
     EITQAEGFRK MLLSVVKDVR VILIKFCDRL HNMRTLDALP EHRRLKIALE TRDIYAPLAH
     RFGLGKMKIE LENLAFKYID PDMFEKVQKK VRLSRGERIA YLDKMIVPIK RDLEKQGFRI
     EAQGRAKHLF SIYNKMRNKN KKFEDIHDLY GIRIIIDTER ISDCFAAYGY ITQKYPPLPQ
     HFKDYISIPK HNGYQSLHSA ILGPKGRVIE VQLRTRRMHE FAEFGVAAHW RYKEKVSKDD
     ASIDSFLKWA RDLINDADSA ASFMEGFKLN LYHEEIYIFT PKGDMKTLPA GSTPIDFAYA
     IHTEIGNGCI GAKVNGKIVR LNSELKSGDR VEIIISKNQK PKVDWLKTVK THRARIKIRS
     AINEERRIQI EKGRNMWDKM LSSTKKLLTE NDIIKQVRKY GIKTPADFFS ALANQQIDGQ
     KVIQSLAEQE HPPFTAEKND DDGLGFDTFA EQARKGREGE LFGKDEVIIE GLPNIAYSYA
     KCCKPVPGDD IIGFVTREGV AKIHRKNCVN VSNKSLLKSE RVVSVAWNRK VETEFLAGVK
     VIGEDRMGIT NHITAVLSKS DINIRSISLH ARDGMFIGTV MIYVRNISRL KALIDKIKKV
     QGVFSVERLS S
//