ID C5CKQ9_VARPS Unreviewed; 747 AA.
AC C5CKQ9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACS19213.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACS19213.1};
GN OrderedLocusNames=Vapar_2587 {ECO:0000313|EMBL:ACS19213.1};
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS19213.1};
RN [1] {ECO:0000313|EMBL:ACS19213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S110 {ECO:0000313|EMBL:ACS19213.1};
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., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA Leadbetter J.R., Spain J.C., Han J.I.;
RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL Submitted (JUN-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; CP001635; ACS19213.1; -; Genomic_DNA.
DR AlphaFoldDB; C5CKQ9; -.
DR STRING; 543728.Vapar_2587; -.
DR KEGG; vap:Vapar_2587; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_4; -.
DR OrthoDB; 9805041at2; -.
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:ACS19213.1}.
FT DOMAIN 418..479
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 676..747
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 575..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 82044 MW; 0B606E4E95FE5CA0 CRC64;
MKRESSSLQT AHASDTAVVD YPLSAATADR TPVMENMLAR ARAFAEPLIA DEKLDTGENT
LAHADAVAAI VAKMGGSEAM QAASYLVYAC QHLNRPQEVI AKVFGDNFAA LAVETTKLVR
VQEQARSASQ GHHLAEGAAG AQTENVRKML LAFSRDLRVV MLRLASRLQT LRHAAASKQP
APESVARESL QVFAPLANRL GIWQVKWEIE DLSFRFLEPE TYKLIARLLD EKRVEREGHV
EQLRSQLERE LQAEGVRATV QGRPKNIYSI VKKMRGKSLD FAQVFDILAL RVVVPDVKDC
YAALAWVHSH FLPIDEEFDD YIARPKPNGY QSLHTVVREM VDGKPGKPIE IQIRTEEMHD
HAEHGVAAHW AYKEAGHKGY AGVWASGEYD AKIAVLRQLL AWERDLSGGS QGQGLFDDRI
YVLTPDAAIV ELPQGATPVD FAYTVHTTLG HRCRGARVDG AMVPLNTPLS NGQTVEIIAA
KEGGPSRDWL NAELGYLASH RARAKVRAWF NAQITHETVA RGREAVEKLL QREGKTSTRL
EDLASQLGFK SADHLFEVVG KDEFSLRNIE VLLRPPEPAP NPDDGVQIKK PRASEKSGKG
GVLVVGVSSL MTQLAKCCKP APPDAIRGFV TRGHGVSVHR VDCSNFRMMA SRDSERVIDV
EWGAAKGGEA PVYAVDVSVE AADRQGLLRD ISDVFAREKM NVIGVQTQSV KGTAWMTFTV
EISDAARLTQ VLGVVTAVAG VRSARRR
//
