ID   SPOT_ECO57              Reviewed;         702 AA.
AC   P0AG25; P17580;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase;
DE            EC=3.1.7.2;
DE   AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE            Short=(ppGpp)ase;
GN   Name=spoT; OrderedLocusNames=Z5076, ECs4525;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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       This enzyme catalyzes the degradation of ppGpp into GDP. It may also be
CC       capable of catalyzing the synthesis of ppGpp (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC         H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58794.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37948.1; -; Genomic_DNA.
DR   PIR; E91194; E91194.
DR   PIR; F86041; F86041.
DR   RefSeq; NP_312552.1; NC_002695.1.
DR   RefSeq; WP_000280488.1; NZ_VOAI01000021.1.
DR   AlphaFoldDB; P0AG25; -.
DR   SMR; P0AG25; -.
DR   STRING; 155864.Z5076; -.
DR   GeneID; 75202219; -.
DR   GeneID; 915518; -.
DR   KEGG; ece:Z5076; -.
DR   KEGG; ecs:ECs_4525; -.
DR   PATRIC; fig|386585.9.peg.4743; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OMA; PIDFAYS; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR006674; HD_domain.
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; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..702
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166570"
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          386..447
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          628..702
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   702 AA;  79342 MW;  A85F70F57D082EE8 CRC64;
     MYLFESLNQL IQTYLPEDQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMK
     LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLKFRD KKEAQAENFR
     KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT
     ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILSEI EGRLQEAGIP CRVSGREKHL
     YSIYCKMVLK EQRFHSIMDI YAFRVIVNDS DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA
     NGYQSLHTSM IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEHGETSTT AQIRAQRWMQ
     SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL PAGATPVDFA YAVHTDIGHA
     CVGARVDRQP YPLSQPLTSG QTVEIITAPG ARPNAAWLNF VVSSKARAKI RQLLKNLKRD
     DSVSLGRRLL NHALGGSRKL NEIPQENIQR ELDRMKLATL DDLLAEIGLG NAMSVVVAKN
     LQHGDASIPP ATQSHGHLPI KGADGVLITF AKCCRPIPGD PIIAHVSPGK GLVIHHESCR
     NIRGYQKEPE KFMAVEWDKE TAQEFITEIK VEMFNHQGAL ANLTAAINTT TSNIQSLNTE
     EKDGRVYSAF IRLTARDRVH LANIMRKIRV MPDVIKVTRN RN
//