SPOT_VIBCH
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 03-AUG-2022, entry version 118.
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; Proteobacteria; 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 OMA; DWISSPK; -.
DR BioCyc; VCHO:VC2710-MON; -.
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; 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; 3.30.460.10; -; 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 Pfam; PF13291; ACT_4; 1.
DR Pfam; PF19296; DUF5913; 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; SSF55021; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00691; spoT_relA; 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
