ID A0A3N4H0R1_9BACT Unreviewed; 740 AA.
AC A0A3N4H0R1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RPA68943.1};
GN ORFNames=EF405_07750 {ECO:0000313|EMBL:RPA68943.1};
OS Cyclobacteriaceae bacterium YHN15.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=2487897 {ECO:0000313|EMBL:RPA68943.1, ECO:0000313|Proteomes:UP000274029};
RN [1] {ECO:0000313|EMBL:RPA68943.1, ECO:0000313|Proteomes:UP000274029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YHN15 {ECO:0000313|EMBL:RPA68943.1,
RC ECO:0000313|Proteomes:UP000274029};
RA Chen Z.;
RT "Cecembia caeni sp. nov.,isolated from a lake.";
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:RPA68943.1}.
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DR EMBL; RKQB01000003; RPA68943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4H0R1; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000274029; 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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RPA68943.1}.
FT DOMAIN 405..466
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 740 AA; 84744 MW; 2A9BE20556762B00 CRC64;
MIQVDLEEER KEILKRYRKL LRTAKPMLKP GDAKIIKKAF SVASEAHKEM RRKSGEPYIY
HPLEVALICV EEIGLGTTSI VSALLHDVVE DTDLELEDIE REFGTKVAQI IDGLTKISGV
FEYGSSQQAE NFRKMLLTLS DDVRVILIKL ADRLNNMRTL ESMPRHKQLK IASETMYLYA
PLAHRLGLYA IKSELEDLYL KYTDTDTYNY IVNKVNETRI SRNKFIKSFL LPIEEELEGQ
GFDFTIKGRP KSVFSIYNKM KKQNIPFEEV YDLFAIRIII DSELEEEKAD CWQVYSIVTD
FYRPNPDRLR DWISTPRSNG YESLHTTVMS NTGQWVEVQI RTVRMDDIAE RGYAAHWKYK
EIEAAQSRSG SGLDEWITQV RTLLESNDGS AIEFMDDFRG NLFHDEVFVF TPKGDLKVLP
FGATALDFAF EIHTEVGAKC IGAKVNQKLV PINHKLKNGD QVEILTSNKQ KPTEDWLNSV
VTSRAKAKIK DALREEKKST IMDGKEIVQR KLRQMKMDFN SEVVEQLRAY FETKTPNEFY
YKVGKGIIDP TSIKSFKDFK EQKKQKSKPT LDKVKDELSF TKEIKNLKGP DHDQLLIGED
MDVVDYILAK CCNPIPGDDV FGFVTVNEGI KIHRTSCPNA LELLSNHGNR VIKARWTSQQ
EIAFLAGLRI VGTDRVGLIN DVTKVISNEL KVNMRSITVD SDSGIFEGTI KLYVHSTQHL
EKLVANLSKV EGIIKVTRFD
//
