ID   SPOT_BORBU              Reviewed;         667 AA.
AC   O51216;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase;
DE            EC=3.1.7.2;
DE   AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE            Short=(ppGpp)ase;
GN   Name=spoT; OrderedLocusNames=BB_0198;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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       This enzyme catalyzes the degradation of ppGpp into GDP. It may also be
CC       capable of catalyzing the synthesis of ppGpp (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AE000783; AAC66590.1; -; Genomic_DNA.
DR   PIR; F70124; F70124.
DR   RefSeq; NP_212332.1; NC_001318.1.
DR   RefSeq; WP_002657610.1; NC_001318.1.
DR   AlphaFoldDB; O51216; -.
DR   SMR; O51216; -.
DR   STRING; 224326.BB_0198; -.
DR   EnsemblBacteria; AAC66590; AAC66590; BB_0198.
DR   GeneID; 56567624; -.
DR   KEGG; bbu:BB_0198; -.
DR   PATRIC; fig|224326.49.peg.594; -.
DR   HOGENOM; CLU_012300_3_0_12; -.
DR   OMA; DWISSPK; -.
DR   UniPathway; UPA00908; UER00886.
DR   PHI-base; PHI:5102; -.
DR   Proteomes; UP000001807; 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; 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; 3.30.460.10; -; 1.
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; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..667
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166568"
FT   DOMAIN          62..161
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          401..462
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
SQ   SEQUENCE   667 AA;  77763 MW;  608AE939725E2120 CRC64;
     MIQAYEIAHL IKINDLEKAR NIFKKTVENT YKDEFERKSI FKALEIAEQL HYGQYRESGE
     PYIIHPIMVS LFLAKFQLDF KATIAGLLHD VLEDTNVEKE EIVKEFDEEI LSLIDGVTKI
     HDLHNKTRSI KEANTISKMF FAMTHDIRII IIKLADKLHN MTTLSYLPKN RQDRIAKDCL
     STYVPIAERL GISSLKTYLE DLSFKHLYPK DYKEIKNFLS ETKIEREKKL YKGKLSIEKE
     LQKSGIEAEI TVRSKHFYSI FRKMQTRTNK LTQIFDTLGI RIICKKQKEC YEILEIVHRV
     WKPIPGRLKD YIASPKENKY QSLHTTVRIP EDNQLIEIQI RTEEMDRIAN YGVAAHWIYK
     EQIELKADDL SFINRIKKWQ QESANKSQYS MNDIHKELLN TFIYVYTPEG EVVELPFGSN
     SIDFAYIIHT DIGDQALYAK INGKISSITK PLKNEQIVEI FTSKDSKPDV IWLNSVRTKK
     ARSKIRSWLN KNDNTIFVDN NIIAYLVGAN KEQRKLFSLF KSYTKTKIKR IAIDPECSPT
     TGEDIIGIIH KDEIIVHNEN CQKLKSYKKP QLIEVEWEAT PTRKVHHIIL LLKELKGIFS
     YLENIFTLND VRLISEKIED CGNGHGITNI IVSSNAKNIT KIISALKENP NILQIMQIEE
     DIKNYDN