ID A0A0W0TK18_9GAMM Unreviewed; 707 AA.
AC A0A0W0TK18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=spoT {ECO:0000313|EMBL:KTC95912.1};
GN ORFNames=Lfee_2274 {ECO:0000313|EMBL:KTC95912.1}, NCTC11978_00844
GN {ECO:0000313|EMBL:STX37676.1}, NCTC12022_01046
GN {ECO:0000313|EMBL:SPX60329.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC95912.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC95912.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC95912.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000251942, ECO:0000313|Proteomes:UP000254033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11978 {ECO:0000313|EMBL:STX37676.1,
RC ECO:0000313|Proteomes:UP000254033}, and NCTC12022
RC {ECO:0000313|EMBL:SPX60329.1, ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; LNYB01000082; KTC95912.1; -; Genomic_DNA.
DR EMBL; UASS01000008; SPX60329.1; -; Genomic_DNA.
DR EMBL; UGNY01000001; STX37676.1; -; Genomic_DNA.
DR RefSeq; WP_058446916.1; NZ_UGNY01000001.1.
DR AlphaFoldDB; A0A0W0TK18; -.
DR STRING; 453.Lfee_2274; -.
DR PATRIC; fig|453.4.peg.2490; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR Proteomes; UP000254033; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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:KTC95912.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698};
KW Transferase {ECO:0000313|EMBL:KTC95912.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 387..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 631..705
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 707 AA; 80028 MW; 9DAA2A591087C163 CRC64;
MSYFKELDEE LKCYLEQPLI EKCYQAYLVA EKAHRGQMRR SGEPYITHPV AAALILARMR
LDYQTIMATL LHDVVEDTSI SKDDLTQQFG EDVTALVDGV TKLTKIKFES RAEAQAENFR
KMVLAMVKDI RVIIVKLADR YHNMRTLGAM PSVKRRRIAI ETLEIYAPIA NRLGMHAIYI
GLEDLGFQAL YPMRYRAIKS AVEKSRGNRR ELTQKIEQDL QQALEKLNIP YEHVFGRQKH
LYSIYRKMRQ KKASFTEITD VFAFRVITED IDSCYRVLGA LHQTYKPVPQ RFKDYIGIPK
ANGYQSLHTT LFGPFGVPLE VQIRTRDMDK VAENGVAAHW IYKSSGLEVN EAQLRAREWV
QRLLEMQRST GNSLEFIENV KIDLFPDEVY VFTPKGHIME LPKGATPVDF AYTVHSGVGN
SCVAAKVNRR LVPLSIPLTN GQTVEIITAP GARPNPAWLN FVVTGKARSN IRHFLKSQQH
TESIVLGKRL LEQSLVELGS DYAKVPPESL QALLHDLNYK SADELLYAIG IGNQMPMIIA
KRLVISQENS ELDKTAKSGP LAIKGTEGMV VHFADCCQPI PGDNIVGRFQ QGRGIIVHAS
DCPNINQGRN HPEQLVSLRW DDQVQGEFWV DITVEVANQR GVLAALATAI SEAESNIGNI
NVDPRDGRHN GVTFSISVRD RTHLARVMRR LRANKVVMRL YRKKQGD
//
