ID   SPOT_VIBCH              Reviewed;         705 AA.
AC   Q9KNM2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=VC_2710;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=17360576; DOI=10.1073/pnas.0611650104;
RA   Raskin D.M., Judson N., Mekalanos J.J.;
RT   "Regulation of the stringent response is the essential function of the
RT   conserved bacterial G protein CgtA in Vibrio cholerae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:4636-4641(2007).
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: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   -!- SUBUNIT: Interacts with CgtA/Obg (AC Q9KUS8) in a yeast 2-hybrid assay.
CC       {ECO:0000269|PubMed:17360576}.
CC   -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. It
CC       can be disrupted in a relA deletion strain (relA phosphorylates GTP to
CC       ppGpp). {ECO:0000269|PubMed:17360576}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF95850.1; -; Genomic_DNA.
DR   PIR; B82044; B82044.
DR   RefSeq; NP_232337.1; NC_002505.1.
DR   RefSeq; WP_010895463.1; NC_002505.1.
DR   AlphaFoldDB; Q9KNM2; -.
DR   SMR; Q9KNM2; -.
DR   DIP; DIP-60892N; -.
DR   IntAct; Q9KNM2; 1.
DR   STRING; 243277.VC_2710; -.
DR   DNASU; 2615538; -.
DR   EnsemblBacteria; AAF95850; AAF95850; VC_2710.
DR   KEGG; vch:VC_2710; -.
DR   PATRIC; fig|243277.26.peg.2585; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   UniPathway; UPA00908; UER00886.
DR   PHI-base; PHI:4167; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IBA:GO_Central.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..705
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000386418"
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          387..448
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          631..705
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   705 AA;  79496 MW;  08F756E3A576B07F CRC64;
     MYLFDSLKDV AQEYLTEPQI EALRQSYVVA RDAHEGQTRS SGEPYIIHPV AVARILAEMR
     LDLETLQAAL LHDVIEDCDV TKEDLDAHFG SSVAELVDGV SKLDKLKFRD RKEAQAENFR
     KMVLAMVQDI RVILIKLADR TPNMRTLGAL RPDKKRRIAR ETLEIYAPLA HRLGIHNIKT
     ELEELGFEAL YPNRYRVLKE VVKAARGNRK EMIQRIHSEI EGRLQEVGLP ARVVGREKNL
     FSIYNKMKTK EQRFHTIMDI YAFRIVVDTA DTCYRVLGQV HSLYKPRPAR MKDYIAVPKA
     NGYQSLHTSM VGPHGVPVEV QIRTEDMDQM ADKGVAAHWS YKANSERGGT TAQIKAQRWM
     QSLLELQQSA GNSFEFIENV KSDLFPDEIY VFTPKGRIVE LPMGATAVDF AYAVHTDIGN
     TCVGARVDRT PYPLSQSLKS GQTVEIISAP GARPNAAWLN YVVTSRARTK IRQVLKTMRR
     EDSITLGRRL LNHALGEHSV NEIAPENISK VLSDLKIASM DDLLAAIGLG ELMSIVIARR
     LLGNADELTE PSKSGGNKNK LPIRGAEGIL LTFANCCHPI PDDHIIAHVS PGRGLVVHRE
     TCPNVRGYQK EPDKYMAVEW TKDYDQEFIT ELKVDMHNRQ GALAELTNVI SKTGSNIHGL
     STEERDGRLY TVTVLLTTKD RVHLAGIMRK IRTMPHALKV RRRKN
//