ID A0A0Q7AX30_9BURK Unreviewed; 758 AA.
AC A0A0Q7AX30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KQW40506.1};
GN ORFNames=ASC76_03525 {ECO:0000313|EMBL:KQW40506.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW40506.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW40506.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40506.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW40506.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40506.1,
RC ECO:0000313|Proteomes:UP000051611};
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:KQW40506.1}.
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DR EMBL; LMDS01000001; KQW40506.1; -; Genomic_DNA.
DR RefSeq; WP_056462403.1; NZ_LMDS01000001.1.
DR AlphaFoldDB; A0A0Q7AX30; -.
DR STRING; 1736528.ASC76_03525; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051611; 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; 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:KQW40506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 79..178
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 420..481
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 683..758
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83930 MW; 9A848A8D70EE2FA0 CRC64;
MTARAPNALR DPAPSAAAGK RAPPSKPLPA AVDAAAASFA ALTHKLDYLD PADTKRVREA
YRFADEAHLG QFRASGEPYI THPIAVAGLC ADWKLDAQAI MAALMHDAME DCGITKIELI
EKFGAPVADL VDGLTKLDKL QFSTREESQA ESFRKMLLAM ARDVRVILIK LADRLHNMRT
MDAMAASKRT RIAGETLEIY APIAHRLGLN QTYRELQELS FQHLRPWRQA ALSKAVQKAR
GYRRDIVERI QHDVERAFLQ AKLPVQVFGR EKTLFSIYKK MREKHLTFAQ VNDIFGFRIV
VADLMQCYMA LGVLHQLFKP LPGRFKDYIA IPKANGYQSL HTTLVSPLGT AVEFQIRTEQ
MHAVAEKGIA AHWLYKSGGA QVQEAQRLGA MWLQSLIDIQ DETHDANEFL EHVKIDLFPD
AVYVFTPKSK ILALPRGATP VDFAYAIHTD VGDHTVAAKV NGEPVALRTE LRSGDVVEIV
STAGARPNPA WLNFVRTGRA RSKIRHYLKN MEQEESRDLG EKMLAQAMRA EGMQLPGSEP
PEATLWQQLT RWSGNKTRDD LFTDIGLGRK IATIVAKRLA RLLAEHGTKP DALTLTMGRY
AADDAAPAQG MVLIDGSEGA SVQLAPCCRP IPGDAIVGYL GRGEGLMVHT VECSVGKRLF
ERDSEHWMSV DWAEQPSRPF ETAVTLLVTN GKGVLAQVAQ AVSEAEADIT HIEMGNEPAA
ETTELQLLLS VRDRLHLADV MRTLKRAPSV QRVARVKP
//
