ID A0A0P7WMY7_9GAMM Unreviewed; 704 AA.
AC A0A0P7WMY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KPQ02233.1};
GN ORFNames=HLUCCO02_06055 {ECO:0000313|EMBL:KPQ02233.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ02233.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ02233.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ02233.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-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:KPQ02233.1}.
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DR EMBL; LIHO01000012; KPQ02233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WMY7; -.
DR STRING; 1298881.Ga0003345_1057; -.
DR PATRIC; fig|1298881.4.peg.1915; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000053932; Unassembled WGS sequence.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KPQ02233.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 386..447
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 630..704
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 195..230
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 704 AA; 80203 MW; 708B580D33C2A311 CRC64;
MYLFEGLKKQ IEAYLPPDSV RKVEEAFHVA FEAHAPQKRA SGEPYITHPV AVTSMLAEMR
LDHETLMAAL LHDVIEDTEK THEDLAEQFG ATVAELVEGV SKLDKLQFNS IEEAQIENYR
KMIMAMVQDI RVILIKLADR THNMRTIEHL RPDKRRRIAR ETLEIYAPLA HRLGIHDIKV
ELEILGFWGL YPWRARLLES EVKRARGNRK AVLERTLEEI QARLEQAGIQ SRVSGREKHL
YSIYRKMLMK ELRFKEVMDI FAFRIVVDSV DTCYRVLGAV HNLYKPIETR FKDYIAIPKS
NGYQSLHTSL KGPHGVPVEI QIRTEEMDLM ADRGVAAHWL YKDAEESGTT AQIRAQKWMQ
SLLELQQSAG NSFEFIENVK SELFPDEIYL FTPDGRIIEL PQGATPVDFA YAVHTDIGNT
CIGARVNNKP YSLSKPLETG QTVEIRTAAG SRPNIAWLNF VVTGKARLKI RQFLKNQQSN
EALLLGERLL RAALGSFRFD DISVEEFKRV AKEMKLDSQD ALLKEIGLGN LMSVAVARRL
VGDHQRLRSA SEGEERGRSL AVKGADGLLL SFAKCCRPIP GDDIIAHVSP GKGLVIHRRE
CKNVRGHEDE PGRYFPVQWD NKPDSQFVSE VRVEIVNHQG ALARLTQVIA ETGCNIQGLK
TEEVDSTIYY IDVAITISNR KHLADVMRRI RKMQHVQRVA RLRK
//
