ID A0A3P2A5T8_9NEIS Unreviewed; 721 AA.
AC A0A3P2A5T8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RRD90226.1};
GN ORFNames=EII21_06240 {ECO:0000313|EMBL:RRD90226.1};
OS Conchiformibius steedae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Conchiformibius.
OX NCBI_TaxID=153493 {ECO:0000313|EMBL:RRD90226.1, ECO:0000313|Proteomes:UP000269923};
RN [1] {ECO:0000313|EMBL:RRD90226.1, ECO:0000313|Proteomes:UP000269923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-280 {ECO:0000313|EMBL:RRD90226.1,
RC ECO:0000313|Proteomes:UP000269923};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRD90226.1}.
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DR EMBL; RQYC01000007; RRD90226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P2A5T8; -.
DR STRING; 1121352.GCA_000620925_01398; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000269923; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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 Hydrolase {ECO:0000313|EMBL:RRD90226.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000269923}.
FT DOMAIN 399..460
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 650..721
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 721 AA; 80580 MW; A9A03B8085ECFB61 CRC64;
MTELRQSYLN YAAAQETSPR RVLENALALA EQHYPADARG TQAGEPLLPR LLSAAQMVAD
MDLLADAVAA TVLTDLPAYA NDWETLISEQ CSPTVCQLVH GIDEVQKLTH FARVDTLATP
EERAQQAEAM RKMLLAMVSD IRVVLIKLAL RTRTMQYLGQ VPDSPATRAL AKETLDIFAP
LANRLGVWQL KWQLEDLGFR HHNPEEYRRI ATLLDEKREE RLEYIDNFLN ILRGEMDKAH
IHYDVAGRPK HIYSIYKKMV KKKLDFDGLY DIRAVRILVD SVAECYSTLG IVHSLWQPIP
GEFDDYIANP KGNGYKSLHT VIVGPEDKGI EVQIRTFEMH EFNEFGVAAH WRYKEGGKGD
SAYEQKIAWL RQLLDWRENM AQSGTEDLAA AFQTELFNDT IYVLTPHGKV LSLPAGATPI
DFAYALHSDL GDRCRGAKVD GQIVPLSTPL ENGQRVEIIA AKSGEPSVNW LHEGWVKSHR
AISKIRAHIR RQNAETIRED GKNRFDKIIA KIHPKPNQQQ LCEKLGFKQL DELYSALGQG
ELTPRAVQKA CETAPPPPPT SPQNIVRKSK IKAGGNGVLI DGEDGLLTNL AKCCKPAPPD
LIAGFITRDR GVSVHRQSCS DFANLSRQHP EKVLPAAWAQ ASAEQVFAIG IEVRAHDRSG
LLRDVSDTLT RHKINVTAVQ TQSRQMEATM RFTLEVKQVD DLPRVLASVA EVKGVTGVVR
L
//
