ID B8J111_DESDA Unreviewed; 719 AA.
AC B8J111;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACL49438.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACL49438.1};
GN OrderedLocusNames=Ddes_1536 {ECO:0000313|EMBL:ACL49438.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49438.1};
RN [1] {ECO:0000313|EMBL:ACL49438.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49438.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL49438.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J111; -.
DR STRING; 525146.Ddes_1536; -.
DR KEGG; dds:Ddes_1536; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_7; -.
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; 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;
KW Transferase {ECO:0000313|EMBL:ACL49438.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 642..716
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 719 AA; 81127 MW; 36B8B61B2F619E75 CRC64;
MIRIQEILDK VSAHNPDADL ELIQKAYVYA ATAHAGQTRL SGEPYLSHPL AVADTLAEMG
FDESTVVAGL LHDTVEDTKA TLEELDENFG EDVADIVDGV TKISMIPFEN KEEAQAENIR
KMILAMSHDM RVLMVKLADR LHNMRTLDFQ KAHKQKGIAQ ETMDIYAPLA NRLGLYIMKR
NLEDLSFKYL RPDIFNQIDH WLDKHQVVEK QIIAKVVDLI KDLLASNGIE GQVYGRIKHK
YSIYKKMQSQ SLTLDEMHDI MAFRVLVKDI RDCYAALGLV HSQWRPVHGR FKDYISMPKT
NGYQSLHTTV IGPEGERIEI QIRTEDMHRQ AEHGVAAHWL YKEKGRVNSK DLEQFGWLRE
IFERQSEETD SREFMHSLKL DLFKDEVYVY TPAGDVKELP EGATPLDFAF IIHTKVGQHC
TGAKINGRLM PLSTELKNGD IVEILTDPSR KPNRDWLKIV KTARARSRIQ RYLRTEERAH
AVSLGRDMLE KEGRKVSLNV NKAIKDGHMA LVAQEMNFES VDDLVASVGY AHTTPRKVLN
RLYAVLHPDA VSSAPETPTV KESKEAAGRK TEGVGISGVD GVLMRFAKCC NPVPGDPIIG
YISRGLGVSV HRADCPNVAN MEPERLISVH WDGAEEKPYE AGIFIIARNE HGVLALVAQV
LAKNNVNITG LNMDNLVDGR AKLRFTVEVR DATQLYQLIE SIRSLPPILE VVRDTEDAQ
//