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Database: UniProt
Entry: D5X0W0_THIK1
LinkDB: D5X0W0_THIK1
Original site: D5X0W0_THIK1 
ID   D5X0W0_THIK1            Unreviewed;       738 AA.
AC   D5X0W0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ADG30756.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:ADG30756.1};
GN   OrderedLocusNames=Tint_1369 {ECO:0000313|EMBL:ADG30756.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG30756.1};
RN   [1] {ECO:0000313|EMBL:ADG30756.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG30756.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-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; CP002021; ADG30756.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5X0W0; -.
DR   STRING; 75379.Tint_1369; -.
DR   KEGG; tin:Tint_1369; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_4; -.
DR   BioCyc; TINT75379:TINT_RS06860-MONOMER; -.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   CDD; cd04876; ACT_RelA-SpoT; 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; 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; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:ADG30756.1}.
FT   DOMAIN          408..471
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          667..738
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   738 AA;  80751 MW;  4202A0B888658BD9 CRC64;
     MSPNQSVTVR SAAQAEPADQ RIDQARAYAL ALIDTVVLET GEPAVEHADG VSAILREIGA
     DADAQAAAYL NLVVPQLAHP QDQLSKHFGE ALAALSVETR KLVEVSRMAR GGPDEAELRR
     RHTELVRRLL LGFSRDLRVA LLRLASRLQS LRYFTRTKQA APAAFLAESM EVYAPLANRL
     GIWQVKWEME DLSFRLMQPE VYKDIARKLD ERRVEREQGI STAISLLQKE LQRQHIAAEV
     VGRPKHIYSI WRKMQGKHLQ FEQVMDLRAL RIIVGDVSAC YAALSVVHAM WASLPGEFDD
     YIAKPKPNGY QSLHTVVRTD SGQIFEIQIR TAAMHAHAEQ GSAAHWAYKE AGAKGYLGQT
     QAGDYQSRIA LARQLLALQQ ELAGASSPAA NAPASTGASA DPAVEADAED RIFVLTPQAR
     IVELARGATP VDFAYALHTD LGHRCRGARV DGALIPLTTP LRSGQTVEIV AAKEGGPSRD
     WLNAELGYLR SPRARAKVRA WFNQLAQQQT IAKGRAQVER LLQREGKTSF NLQSLAEGLG
     FRTADELFER VGKDEFSQRQ IEAYLRADPA TSAADESLVF SSGGAAPKKQ GGQVLVVGMG
     SLLTQLAACC KPAPPDAIGG FVTREKGVTV HRANCQNFRN IARQHPERVI AVTWAGQDDA
     SALYPIDLEV SATDRQGLLR DISDVLTQER INVIAVSTRS VGDLAQMRFT VQLANSAKLK
     RALKLIADVP GVLKASRK
//
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