ID A0A0Q6B7C8_9PROT Unreviewed; 738 AA.
AC A0A0Q6B7C8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KQT41346.1};
GN ORFNames=ASG34_11415 {ECO:0000313|EMBL:KQT41346.1};
OS Methylophilus sp. Leaf416.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT41346.1, ECO:0000313|Proteomes:UP000050891};
RN [1] {ECO:0000313|EMBL:KQT41346.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41346.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT41346.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41346.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT41346.1}.
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DR EMBL; LMQS01000004; KQT41346.1; -; Genomic_DNA.
DR RefSeq; WP_055830605.1; NZ_LMQS01000004.1.
DR AlphaFoldDB; A0A0Q6B7C8; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000050891; 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; 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; 2.
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:KQT41346.1}.
FT DOMAIN 70..169
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 655..730
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 83575 MW; 3B2C2D2F650B08C5 CRC64;
MPHTQGEHSY RKSKSPLEAA DLLPADREDS PLTQLIRKYL NEEEVQLVWQ AYRYAEQAHA
GQTRKTGEPY ITHPISVACI LAKLHLDLPT LLAALLHDVV EDTEVNSAEI AEKFGKQVAD
LVDGLTKLDK VELQTATQAQ AENFRKMLLA MSQDVRVILV KLADRLHNMQ TMDAMRPEKQ
KRIARETLDI YAPIANRLGL NPIFHELEDL SLKYLYPNRY RVIDKAIRTA RGNRKEVIGK
ILESIQNQLK QYQLEFNVEG REKHLYSIYK KMSEKSMKLS QIGDIYGFRV VVKDTAACYL
ALGALHALYK PIPGRFKDYI AIPKANGYQS LHTTLFGPFG TPIEVQIRSQ EMHNIADAGV
AAHWLYKTTD AHLTKLQQQT HQWLQRLVEI QTESDDSHEF LENFKVDLFP DEVYIFTPKG
NIMALPRGST AVDFAYAVHS DVGNSCVAVK INNELAPLRT EMRNGDHVEI ITAPLAKPNP
AWLNYVVTGK ARSHIRHYLK TVKVEESAQL GERMLNVALR AMHIQPGDIS DKQWQKVMND
YGAKTRQMIL TDIGLGKRNS LMVAHQLLAH PADTEDKTSK TLDTITIRGS EGMAVQFAPC
CRPIPGDPIL GFINKDKGLV IHTHDCQAIR KFKLDPEKWL DVEWDADPKK LFSVNLRISV
VDERGMLAKI AATIANADAN IDNVSVESSD GSQYSNVNFT LQVHNRVHLA TLIRNLRKIQ
QVVRINRVKG NQLEQRIQ
//
