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Database: UniProt
Entry: A0A0J5GE45_9NEIS
LinkDB: A0A0J5GE45_9NEIS
Original site: A0A0J5GE45_9NEIS 
ID   A0A0J5GE45_9NEIS        Unreviewed;       720 AA.
AC   A0A0J5GE45;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KMJ52557.1};
GN   ORFNames=ACG97_12925 {ECO:0000313|EMBL:KMJ52557.1};
OS   Vogesella sp. EB.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ52557.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ52557.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ52557.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT   Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) 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:KMJ52557.1}.
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DR   EMBL; LFDT01000024; KMJ52557.1; -; Genomic_DNA.
DR   RefSeq; WP_047967783.1; NZ_LFDT01000024.1.
DR   AlphaFoldDB; A0A0J5GE45; -.
DR   STRING; 1526735.ACG97_12925; -.
DR   PATRIC; fig|1526735.3.peg.2770; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000054352; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase 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; 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; 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; 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   Hydrolase {ECO:0000313|EMBL:KMJ52557.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054352}.
FT   DOMAIN          61..160
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          402..463
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          645..720
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   720 AA;  79972 MW;  4074FA66E934CC6C CRC64;
     MSQDSAAEHI DYNALVDAEA AALFDAANQY LRPEDVQLLR QAFATAREAH EGQTRKSGEP
     YITHPLAVAA MLTDWRLDAQ GLAAALMHDV LEDTGVSKPT LSEKFGRTIA DLVDGLSKLE
     RLEYQTKESA QAENFRKMVL AMARDIRVII VKLADRLHNM RTLDAMREDK RQRIALETLE
     IYAPIANRIG LNKVYRELQD LAFKHLHPHR YSVLSKAVRA ARGNRREVVN KILQAVTQKL
     GEANIEATIK GREKNLYSIY KKMQEKHLSF SEVLDIYGFR IVVKDNASCY LTLGALHSLY
     KPIPGKFKDY IAIPKGNGYQ SLHTTLFGPY GTPVEMQIRT QEMNAVAEAG VASHWMYKSG
     DASIDAAKQR THQWLQSILD MQEESEDAIE FLEHIKIDLF PDEVYVFTPK GKIMVLPQGS
     TPVDFAYAVH TDIGHRCIAG RVNFNLVPLR TVLRNGDTVE IITSTQAKPN PSWLNFVQSG
     RARSGIRNYL KTLQQKDAVQ LGEKLLRQAA SALSPTPLDI SPKLEDSLLH ALGERQRSFN
     DLLADIGTGK QLAIVIARKL FELSGEQLGQ TPDVGPVTIR GNEGGAVQLS SCCNPIPGDA
     IIGAISKGQG LLVHRKGCGN AARIDPEKLL EVNWEPQKDR MFGVNISVLA HNQRGALAEI
     AAAISQASAN IETVDTQENH GGDGFIHIHF RLQVDNLIHL ENVLTAIQQV NVVQQAERRQ
//
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