ID   SPOT_MYCGE              Reviewed;         720 AA.
AC   P47520; Q49221;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable 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=MG278;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-224.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71500.1; -; Genomic_DNA.
DR   EMBL; U01770; AAD10588.1; -; Genomic_DNA.
DR   PIR; G64230; G64230.
DR   RefSeq; WP_009885909.1; NZ_AAGX01000009.1.
DR   AlphaFoldDB; P47520; -.
DR   SMR; P47520; -.
DR   STRING; 243273.MG_278; -.
DR   EnsemblBacteria; AAC71500; AAC71500; MG_278.
DR   KEGG; mge:MG_278; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_0_0_14; -.
DR   OMA; YEAINFK; -.
DR   OrthoDB; 204079at2; -.
DR   BioCyc; MGEN243273:G1GJ2-336-MON; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000000807; 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   Gene3D; 3.30.460.10; -; 1.
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   Pfam; PF04607; RelA_SpoT; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..720
FT                   /note="Probable guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166572"
FT   DOMAIN          49..154
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   CONFLICT        219..224
FT                   /note="YDNEWD -> LWQWVG (in Ref. 2; AAD10588)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   720 AA;  84139 MW;  285A6E8670FD8A12 CRC64;
     MATIQEIECD FLAKIAQKFT NAEIELINKA FYHAKTWHEN QKRLSGEPFF IHPLRTALSL
     VEWNMDPITI CAGLLHDIIE DTDQTEANIA MIFSKEIAEL VTKVTKITNE SKKQRHLKNK
     KENLNLKSFV NIAINSQQEI NVMVLKLADR LDNIASIEFL PIEKQKVIAK ETLELYAKIA
     GRIGMYPVKT KLADLSFKVL DLKNYDNTLS KINKQKVFYD NEWDNFKQQL KKILAQNQIE
     YQLESRIKGI YSTYKKLTVH EQNISKIHDL FAIRLITKSE LDCYHILGLI HLNFLIDSKY
     FKDYIASPKQ NLYQSIHTTV RLKGLNVEIQ IRTQQMDNVS KFGLASHWIY KEQKEGLLAP
     ALQLNYLVTK QKHSHDFLKR IFGTDIIKIN VSASHEPNVI KQINVDSNNK LLDIAFENYP
     KQFAKLTKIE IDGVEINSFD TSVENEMLIE FYFGKNNNLK SKWIRYMNNP IYREKVKKSL
     AKLAKSGRYS ELAFYEKELG EKQLKLASET EIQKRLNTLR IKKMSDYLAL IECTNFTNDE
     HLLFLAKNND KWNKLTKPLK FAFSKVVFHN SYFEQIEGIF ITKIVIEPCC SKIPDMPEQV
     TGILTKNILS VHRYGCKNLQ NKKQLKIIPL YWNIQQLKLK PRKFRSYINI NGVWSEKTIN
     KICQTIINGD GYIEKIIPKI NKQKDEFDLN ITLFVNNYQQ LLTLMDQITT KNISFSWKYL