ID A0A0W0WKY8_9GAMM Unreviewed; 707 AA.
AC A0A0W0WKY8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:KTD32994.1};
GN ORFNames=Lnau_2642 {ECO:0000313|EMBL:KTD32994.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD32994.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD32994.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD32994.1,
RC ECO:0000313|Proteomes:UP000054725};
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.
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:KTD32994.1}.
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DR EMBL; LNYO01000024; KTD32994.1; -; Genomic_DNA.
DR RefSeq; WP_058505627.1; NZ_LNYO01000024.1.
DR AlphaFoldDB; A0A0W0WKY8; -.
DR STRING; 45070.Lnau_2642; -.
DR PATRIC; fig|45070.6.peg.2788; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:RHEA.
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:KTD32994.1};
KW Transferase {ECO:0000313|EMBL:KTD32994.1}.
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; 80069 MW; 7BB1E077B15C632C CRC64;
MSYFKELDEE LKCYLEQPLI EKCYQAYLVA EKAHHGQMRR SGEPYITHPV AAALILARMR
LDYQTIMATL LHDVVEDTSI SKDDLTQQFG EDVTALVDGV TKLTKIKFES RAEAQAENFR
KMVLAMVKDI RVIIVKLADR FHNMHTLGAM PAVKRRRIAI ETLEIYAPIA NRLGMHAIYT
GLEDLGFQAL YPMRYRAIKS AVEKSRGNRR ELTQKIEQDL QEALHELNIP YEHVFGRQKH
LYSIYRKMRQ KKASFTEITD VFAFRVITED IDSCYRVMGA LHRTYKPVPQ RFKDYIGIPK
ANGYQSLHTT LFGPFGVPLE VQIRTRDMDK VAENGVAAHW IYKSSGLEVN EAQLRAREWV
QRLLEMQRST GSSLEFIENV KIDLFPDEVY VFTPKGHIME LPKGATPVDF AYTVHSGVGN
SCVAVKVNRR LVPLSIPLTN GQTVEIITAP GAHPNPAWLN FVVTGKARSN IRHFLKSQQH
AESIVLGKRL LEQSLTELTS DYAKVPPETL QALLHDLSYK SADELLYAIG IGNQMPMVIA
KRLVSTQDMA ELDKTARSRP LAIKGTEGMV VHFADCCQPI PGDNIVGRFQ QGRGIIVHAS
DCSNINQGRS HPDQLISLRW DEQVEGEYWV DITVEVANQR GVLAALATAI SEAESNIGNI
NVDPRDGRHN AVTFSISVRD RSHLARVMRR LRANKVVMRL YRKKQGD
//
