ID B4EZA4_PROMH Unreviewed; 708 AA.
AC B4EZA4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
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:CAR45640.1};
GN OrderedLocusNames=PMI2864 {ECO:0000313|EMBL:CAR45640.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR45640.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR45640.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR45640.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45640.1; -; Genomic_DNA.
DR RefSeq; WP_004246819.1; NC_010554.1.
DR AlphaFoldDB; B4EZA4; -.
DR EnsemblBacteria; CAR45640; CAR45640; PMI2864.
DR GeneID; 6799887; -.
DR KEGG; pmr:PMI2864; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000008319; Chromosome.
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 Hydrolase {ECO:0000313|EMBL:CAR45640.1}.
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 634..708
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 708 AA; 80363 MW; CD4AF1D5209B0628 CRC64;
MYLFESLNQI VQKYLPPEQV EQLKKAFIVA RDAHEGQTRS SGEPYITHPV AVACILADMR
LDHQTLMAAL LHDVIEDTPA TFKDIETLFG STVADLVEGV SKLDKLKFRD KKEAQAENFR
KMIMAMVKDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT
ELEELGFEAL HPNRYRVIKE VVKAARGNRK EMINKILSEI EGRLTEASIQ CKVNGREKHL
YSIYRKMLLK EQRFHSIMDI YAFRVIVKDV DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA
NGYQSLHTSL IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEQGEQPGT TAQVRAQRWM
QSLLELQQSA GSSFEFIENV KSDLFPDEIY VFTPEGRIVE LPTGATPVDF AYAVHTDIGH
ACVGARVDRQ PYPLSQSLRT GQTVEIITAP GARPNAAWLN FVVSSRARSK IRQLLKNLKR
EDSINLGRRL LNHALGHHKV ADIPLENIER ELKRMKLHSM DDIMAEIGLG NAMSVVVARN
LLIDNQQQEE HTHLSITNDE TPKLPIKGAD GVLISFAKCC RPIPGDPIVA HISPGKGLVI
HHESCRNIRG YQKEPEKFMP VEWDKDIDGD FITEIKVDMI NHQGALANLT AAINDANSSI
QSMNTEEKDG RVYCAFIRLT AKDRIQLANI MRKLRIMPDV LRVSRNKN
//
