ID   SPOT_MYCPN              Reviewed;         733 AA.
AC   P75386;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=MPN_397; ORFNames=MP441;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96089.1; -; Genomic_DNA.
DR   PIR; S73767; S73767.
DR   RefSeq; NP_110085.1; NC_000912.1.
DR   RefSeq; WP_010874753.1; NC_000912.1.
DR   AlphaFoldDB; P75386; -.
DR   SMR; P75386; -.
DR   IntAct; P75386; 4.
DR   STRING; 272634.MPN_397; -.
DR   EnsemblBacteria; AAB96089; AAB96089; MPN_397.
DR   KEGG; mpn:MPN_397; -.
DR   PATRIC; fig|272634.6.peg.428; -.
DR   HOGENOM; CLU_012300_0_0_14; -.
DR   OrthoDB; 9805041at2; -.
DR   BioCyc; MPNE272634:G1GJ3-630-MONOMER; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000000808; 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; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 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   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; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..733
FT                   /note="Probable guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166573"
FT   DOMAIN          62..167
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   733 AA;  86404 MW;  8F45E41A34BB3940 CRC64;
     MFYNWLKLYK FSKMATLVEI ERDFLQKTAQ KFAPEVVALI TKALDYSKKW HGEQKRLSGE
     PFFIHPLRTA LRLVEWNMDS NTVCAGLLHD IIEDTQVTEA DLTAIFGKEI TDLVVKVTKI
     TSESKKQRQL NRKKEDLNLK SLVNIAMSSQ QEVNALVLKL ADRLDNISSI EFLAVEKQKI
     IAKETLELYA KIAGRIGMYP VKTQLADLSF KVLDPKNFNN TLSKINQQKV FYDNEWGNFK
     KQLEEMLEQN QIEYRLESRI KGIYSTYQKL TFHEQNIAKI HDLFAIRLIV KSELDCYHLL
     GLIHLNFTVL MKHFKDYIAS PKQNFYQSIH TTVRLKGLNV EIQIRTQRMD HVSKYGFASH
     WIYKEKKEGL LASALQVNYL NSKQMHSRDF FKRIFGTDII KVNVSSDNEP NIVKKLNVES
     NSKLLDIAYE LYPKQFNKLE KIKLDGVEVM SFDVTAENEM VIEFCFGKTN NLKRRWLRYM
     NNHVFRERVK KDLNKLKKAV KYSELPLYEK ALEELHLKLA DETQIKQRLN ALGIKKLTEF
     LELIEYPHFP KNEHLYFLAS NNQKWRELIK PIKFALSQAV FQNSYFEQIE GIYITKIVIE
     TCCTKIPDMP EQVIGILMKN ILRVHLHDCR ELANQKQPKI IPLYWNAHQL KMRPRKFRCQ
     INIRGVWSET TVNKIVQTII EGDSYLERII PKIDKQKDEF ELNITMFIDN YHQLITIMEQ
     ITTKNISYVW KYL
//