ID A0A3P1W2F5_9FUSO Unreviewed; 721 AA.
AC A0A3P1W2F5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RRD39946.1};
GN ORFNames=EII29_05345 {ECO:0000313|EMBL:RRD39946.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD39946.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD39946.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD39946.1,
RC ECO:0000313|Proteomes:UP000280115};
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:RRD39946.1}.
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DR EMBL; RQYW01000006; RRD39946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1W2F5; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000280115; 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; 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; 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; 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; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RRD39946.1}.
FT DOMAIN 48..145
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..444
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 721 AA; 84394 MW; 3240D8115385E2CE CRC64;
MEERKLLQRL INKIKENNLD IDIEKIVEAY TLAAESHVGQ KRRSGEDYIL HPVEVAEILV
DMKMDTDTVI AGILHDVVED TLITLPDIEY SFGKDVSRLV DGVTKLRNLP KTDSKKIENI
RKMVVAMSED IRVVIIKLAD RLHNMRTLKY MSSEKQEIKS KETLEIYAPI AHRIGMAKIK
WELEDISFRY LYPKDYKEIS DLVNSKREER EEYTSDIIRK IDRELKRHHV KSEVTGRPKH
LYSIYRKMYE KEKKFADLND LIAIRIIVDK EEECYNVLGI IHNLFVPVSG RFKDYIAVPK
SNGYQSIHTT VKGPKDQNVE IQIRTFEMHR IAEEGVAAHW KYKEKKSKSK NEEYYAAVKK
MIETNSENPE KFARTITGSL LNQTIFIFTP KGDVMELAND STALDFAFQV HTQIGYRTIG
AKVNDRIVQL DHLLENGDKV EILTSRNTKG PGKDWINMVN NHSSKVKIRK WFKDKEFEEK
TKEGEQLLER EFEKLGIKLK DLEEDERVFL YMKKFNISTM DLLFYKFAVG DLSLDGFLNK
FEVKEEKDIK QVLEEETEKG NRRKEKSHGG VRISGTENTM YRFAKCCSPL PGDEIRGYVT
RGRGIAIHRS DCENFHTLME HEPDREIEVF WDEEEVNSSI AKYQFNFTVK AVDRNGMLLD
IIRILNEYKM ELINVNTNYV KENGNRYVLL HFGIMIRKRE DFERLANNLI SMKDVVDILR
K
//
