ID Q2SY70_BURTA Unreviewed; 789 AA.
AC Q2SY70;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Guanosine-3`,5`-bis(Diphosphate) 3`-pyrophosphohydrolase {ECO:0000313|EMBL:ABC37802.1};
GN OrderedLocusNames=BTH_I1588 {ECO:0000313|EMBL:ABC37802.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC37802.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC37802.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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}.
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DR EMBL; CP000086; ABC37802.1; -; Genomic_DNA.
DR RefSeq; WP_009889758.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SY70; -.
DR GeneID; 66547972; -.
DR KEGG; bte:BTH_I1588; -.
DR HOGENOM; CLU_012300_3_0_4; -.
DR Proteomes; UP000001930; Chromosome I.
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; 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 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"
SQ SEQUENCE 789 AA; 88062 MW; 0C95870FA169B0A8 CRC64;
MSTTPSSASS EAGHAEAAAP SHARQYIDAV LEQSFRHLFG PTATPEQPRK HGVVSIAKLT
AALADYLSPE EIKEVKAAFH FSDEAHLGQY RQSGEPYITH PVAVAEICAG WKLDAQAIMA
ALLHDVMEDQ GVTKSELAER FGPKVAELVD GLSKLDKMEF RSREEAQAEN FRKMLLAMAR
DVRVILVKLA DRLHNMRTLG AVPMEKRRRV ARETLDIYAP IAHRLGLNNT YRELQDMSFA
NFNPHRYATL EKAVKAARGN RREVIGKILE SVQRAMADAK IDAEITGREK TIYSIYKKMR
DKQLSFSQVL DVYGFRIVVE HPLDCYTCIG VLHALYKPVP GKFKDYIAIP KVNGYQSLHT
TLVGPFGAPI EFQVRTRKMH EIAEAGVAAH WLYKNGGADL NDVQKRAHQW LKSLLDIQSE
AGDSSEFLEH VKIDLFPDAV YVFTPKSKIM ALPRGATALD FAYSIHSDLG NQCVAVKINN
ELLPLRTELK SGDIVEVITA PYSKPNPAWL GFVRTGKARS AIRHYLKTMR LNESVQLGER
LVDQSLKGYG LALADVTPEV WEKLVQWTGN KSRQEIFADI GLGRRVAAVM AKRIEVLMSG
RDADDDLPRA ERQATNHAPP VVITGTEGMS VQLSACCRPI PGDDIMGYIG IGLGMAIHTT
ACRVAQRIHR RDPGRWIDVA WAPQPGRLFD VAVKALVKNT KGIFARVAAD ITSADANIVH
IAMDEDLTQE STVLRFVIQV SDRVHLANVM RRVRTNPDVM RIMRERSSDD VVHARHDGGM
RIDRERQDY
//
