ID A0A069P6X8_9BURK Unreviewed; 789 AA.
AC A0A069P6X8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KDR36435.1};
GN ORFNames=BG57_16375 {ECO:0000313|EMBL:KDR36435.1};
OS Caballeronia grimmiae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1071679 {ECO:0000313|EMBL:KDR36435.1, ECO:0000313|Proteomes:UP000027439};
RN [1] {ECO:0000313|EMBL:KDR36435.1, ECO:0000313|Proteomes:UP000027439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R27 {ECO:0000313|EMBL:KDR36435.1,
RC ECO:0000313|Proteomes:UP000027439};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-2014) 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 -!- 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:KDR36435.1}.
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DR EMBL; JFHE01000003; KDR36435.1; -; Genomic_DNA.
DR RefSeq; WP_035961107.1; NZ_JFHE01000003.1.
DR AlphaFoldDB; A0A069P6X8; -.
DR STRING; 1071679.BG57_16375; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000027439; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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:KDR36435.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}.
FT DOMAIN 97..196
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 438..499
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 692..767
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 764..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 88499 MW; 064B0D6CD50F1EA3 CRC64;
MDPETDSDID QDALLDADKP HAARKYIDAV LEQSFRHLFG PTATPEQPRK HDVVSIANLT
NALASYISAD EIKEVKAAFH FSDEAHLGQY RQSGEPYITH PVAVAEICAS WKLDAQSIMA
ALLHDVIEDQ GVTKTEIAER FGAKVAELVD GLSKLDKMEF RNREEAQAEN FRKMLLAMAR
DVRVILVKLA DRLHNMRTLG AVPPEKRRRV ARETLDIYAP IAHRLGLNNT YRELQDLSFA
NFNPNRYATL EKAVKSARGN RREVVGKILE AVQRTIADAK ICAEVTGREK TIFSIYKKMR
DKQLSFSQVL DVYGFRVVVE SALECYTCIG ALHALYKPVP GKFKDYIAIP KVNGYQSLHT
TLVGPFGAPI EFQIRTRKMH EIAEAGVAAH WLYKNGGADL NDVQKRAHQW LKSLLDIQSE
AGDSSEFLEH VKIDLFPDAV YVFTPKSKIM PLPRGATALD FAYSIHSDLG NQCVAVKINN
ELLPLRTELK SGDIVEVITA PYSKPNPAWL GFVRTGKARS AIRHYLKTMR LNESVQLGER
LVDQSLKGYG LALSEVTPEV WEKLVQWTGN KTRQEIFADI GLGRRVAAVM AKRIEVLMNG
IADDDEHPHR EHHNTNTAPP VVITGTEGMS VQLSPCCRPI PGDNIMGYIG IGLGMAIHTT
ECRVAQRIHR RDPGRWIDVA WAPQPGRLFD VAVKVLVRNT KGVFARVAAD ITSADANIVH
IAMDEDVSQE AKLLRFVIQV SDRVHLANVM RRVRTNLDVM RIARERPSDE PHHRNQDGGM
RVDRERADY
//
