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Database: UniProt
Entry: U3BJ26_VIBPR
LinkDB: U3BJ26_VIBPR
Original site: U3BJ26_VIBPR 
ID   U3BJ26_VIBPR            Unreviewed;       706 AA.
AC   U3BJ26;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE            EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN   Name=spoT {ECO:0000313|EMBL:GAD66653.1};
GN   ORFNames=VPR01S_04_02570 {ECO:0000313|EMBL:GAD66653.1};
OS   Vibrio proteolyticus NBRC 13287.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD66653.1, ECO:0000313|Proteomes:UP000016570};
RN   [1] {ECO:0000313|EMBL:GAD66653.1, ECO:0000313|Proteomes:UP000016570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD66653.1,
RC   ECO:0000313|Proteomes:UP000016570};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA   Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL   Submitted (SEP-2013) 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   -!- 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         Evidence={ECO:0000256|ARBA:ARBA00024273};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC       1/1. {ECO:0000256|ARBA:ARBA00024329}.
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:GAD66653.1}.
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DR   EMBL; BATJ01000004; GAD66653.1; -; Genomic_DNA.
DR   RefSeq; WP_021704631.1; NZ_BATJ01000004.1.
DR   AlphaFoldDB; U3BJ26; -.
DR   STRING; 1219065.VPR01S_04_02570; -.
DR   eggNOG; COG0317; Bacteria.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000016570; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 {ECO:0000313|EMBL:GAD66653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016570}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          387..448
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          632..706
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   706 AA;  79880 MW;  83F1ECBCD4546C00 CRC64;
     MYLFDSLKDV AQEYLTEPQI EALRQSYVVA RDAHEGQTRS SGEPYIIHPV AVARILAEMR
     LDIETLQAAL LHDVIEDCDV TKEELESQFG ATVAELVDGV SKLDKLKFRD RKEAQAENFR
     KMVLAMVQDI RVILIKLADR THNMRTLGAL RPDKKRRIAR ETLEIYSPLA HRLGIHNIKT
     ELEELGFEAL YPNRYRVLKE VVKAARGNRK EMIQRIHLEI EGRLQEVGLK ARVFGREKNL
     FSIYNKMKSK EQRFHTIMDI YAFRVVVDDA DTCYRVLGQV HSLYKPRPGR MKDYIAVPKA
     NGYQSLHTSM VGPHGVPVEV QIRTEDMDQM ADKGVAAHWS YKDKGDKSGT TAQIKAQRWM
     QSLLELQQSA GNSFEFIENV KSDLFPDEIY VFTPKGRIVE LPVGATAVDF AYAVHTDVGN
     TCVGARVDRN PYPLSKALKN GQTIEIISAP GARPNAAWLN YVVTSRARTK IRQVLKTMRR
     EESITLGRRL LNHALGEKSL SDISDDNIQH VLTDLKIGST DDLLAAIGLG ELMSIVIARR
     LLGNADELTE VMGKDGQPKK KLPIRGAEGI LLTFANCCHP IPDDHIIAHV SPGRGLVVHR
     ETCPNVRGYQ REPDKYMAVE WSRDYDQEFI TELLVDMQNR QGALAELTNV ISQTGSNIHG
     LSTEERDGRL YTVTVALTTK DRVHLASIMR KIKAMPQTLK VRRRKH
//
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