ID A0A1Q8TF35_9GAMM Unreviewed; 711 AA.
AC A0A1Q8TF35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=BTW10_04855 {ECO:0000313|EMBL:OLO12238.1};
OS Chromohalobacter japonicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=223900 {ECO:0000313|EMBL:OLO12238.1, ECO:0000313|Proteomes:UP000186806};
RN [1] {ECO:0000313|EMBL:OLO12238.1, ECO:0000313|Proteomes:UP000186806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB17 {ECO:0000313|EMBL:OLO12238.1,
RC ECO:0000313|Proteomes:UP000186806};
RA Mavrodi D.V., Olsson B.E., Korsakova E.S., Pyankova A., Mavrodi O.V.,
RA Plotnikova E.G.;
RT "Draft genome sequences of strains Salinicola socius SMB35, Salinicola sp.
RT MH3R3-1 and Chromohalobacter sp. SMB17 from the Verkhnekamsk potash mining
RT region of Russia.";
RL Submitted (DEC-2016) 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 -!- 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:OLO12238.1}.
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DR EMBL; MSDQ01000007; OLO12238.1; -; Genomic_DNA.
DR RefSeq; WP_075368449.1; NZ_MSDQ01000007.1.
DR AlphaFoldDB; A0A1Q8TF35; -.
DR STRING; 223900.GCA_000821045_00680; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000186806; 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:OLO12238.1};
KW Transferase {ECO:0000313|EMBL:OLO12238.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 389..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 637..711
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 711 AA; 79679 MW; A98FE6C2A141D30E CRC64;
MFTIDDLADR LGGYLPPEEI LHVKRAFYYA EQAHDGQRRR SGEPYVTHPL AVANILANMH
MDHQSLMAAM LHDVIEDTGV TKEALTQQFG EPVAELVDGV SKLTQITFED KAVAQAENFQ
KMVLAMSQDI RVIIVKLADR LHNMRTLGAL RPDKKRRIAR ETLEIYARIA GRLGINTIRV
ELEDLSFQAI HPMRAERIKR AVTKARGNRR SMMRQIQDSL QKCLDDDALG GSVVGRQKHL
LSIYRKMRDQ RKPFAEIMDV FGFRIITDDV DTCYRILGAV HNLYKPVPGR FKDYIAIPKA
NGYQSLHTTL FGPSGMPVEV QIRTREMEAM ANNGIAAHWL YKAGQTERPI GAGSHARARE
WVRGLLEMQR HAGNSLEFIE HVKNDLFPDD IYVFTPKGDI MELPGGATAV DFAYSVHTDI
GNSCIACRID RHLAPLSSTL ESGQTLEIIT APGARPNLAW LNFVVTAKAR SAIRHALKHQ
QRTESVQLGR RLLNRALSAF ETSLEELPEH RLAAILEELD LKHEDDLLES IGLGTRMAYA
IARRLLECNA PETAEEVATA SRSGMPIVIN GAEGMIISFA RCCYPLPGDP IVGHLSVGKG
IVVHRHDCGN LRELRDDPDK LFALEWSQQI DQDFPVALRL HVETRRGLVA ELAGLVTDAD
ANIERIGIEE RDARLSIVNL TLAVHDRVHL ASIMKRLRNL PHVGKITRVR S
//
