ID A0A1E5E704_9VIBR Unreviewed; 709 AA.
AC A0A1E5E704;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=A1QC_03560 {ECO:0000313|EMBL:OEF30078.1};
OS Vibrio rumoiensis 1S-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF30078.1, ECO:0000313|Proteomes:UP000094070};
RN [1] {ECO:0000313|EMBL:OEF30078.1, ECO:0000313|Proteomes:UP000094070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1S-45 {ECO:0000313|EMBL:OEF30078.1,
RC ECO:0000313|Proteomes:UP000094070};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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:OEF30078.1}.
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DR EMBL; AJYK02000003; OEF30078.1; -; Genomic_DNA.
DR RefSeq; WP_017025404.1; NZ_AJYK02000003.1.
DR AlphaFoldDB; A0A1E5E704; -.
DR STRING; 1188252.A1QC_03560; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000094070; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:OEF30078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094070};
KW Transferase {ECO:0000313|EMBL:OEF30078.1}.
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 635..709
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 709 AA; 80121 MW; F8051F951956DB8F CRC64;
MYLFESLKAV AQEYLPESQL ETLSEAFVVA RDAHEGQSRS SGEPYIIHPV AVARILAEMH
LDNETLMAAL LHDVIEDTEV TKEDLANQFG ETVAELVDGV SKLDKLKFRD RKEAQAENFR
KMILAMVQDI RVILIKLADR THNMRTLGAL RPDKRRRIAR ETLEIFSPLA HRLGIHNIKT
ELEELGFEAL YPNRYRVLKE VVKAARGNRK EMIQRIHSEI EGRLLDVGLK VRVLGREKNL
YSIYNKMRSK EQRFHTIMDI YAFRVIVDTP DTCYRVLGQV HNLYKPRPSR MKDYIAVPKA
NGYQSLHTSM VGPHGVPVEV QIRTEDMDQM ADKGVAAHWS YKAHGESSGT TAQIKAQRWM
QSLLELQQSA GNSFEFIENV KSDLFPDEIF VFTPKGRIIE LPAGATAVDF AYAVHTDVGN
TCVGSRVDRN PYPLSKSLKN GQTIEIISAP GARPNAAWLN YVVTSRARTK IRQVLKTMRR
EESVALGRRL LNHALGEQSI SDISQENIQH VLSDLKLKSI DELLAAIGLG ELMSIVIARR
LLGDADELTE MDSPDDHSSS SKKKLPIRGA EGILLTYAKC CHPIPGDHII AHVSPGRGLV
VHRETCPNIR GYQKEPERYM AVEWSKDFDQ EFITELKVDM QNRQGALADL TNVVASTGSN
IHGIATEERD GRLYTISLLL TTKDRVHLAS IMKRIRVMPH TLKVRRSRN
//
