ID   SPOT_SPICI              Reviewed;         749 AA.
AC   O34098;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 105.
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;
OS   Spiroplasma citri.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GII-3;
RX   PubMed=9244268; DOI=10.1128/jb.179.15.4802-4810.1997;
RA   Jacob C., Nouzieres F., Duret S., Bove J.M., Renaudin J.;
RT   "Isolation, characterization, and complementation of a motility mutant of
RT   Spiroplasma citri.";
RL   J. Bacteriol. 179:4802-4810(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; U89875; AAC45548.1; -; Genomic_DNA.
DR   AlphaFoldDB; O34098; -.
DR   SMR; O34098; -.
DR   STRING; 2133.SCITRI_00787; -.
DR   UniPathway; UPA00908; UER00886.
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; 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; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   Pfam; PF13291; ACT_4; 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; SSF55021; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..749
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166575"
FT   DOMAIN          49..148
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          407..468
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          674..749
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   749 AA;  86282 MW;  D32992E612317042 CRC64;
     MDRDIKYEEV LAQIKLYIKD EATLKEIQKA YEYAEEKHHG QVRNSGARYI IHPLWTTFFL
     AQWRMGPKTL IAGLLHDVLE DTPATFEELQ ELFGIEIANL VEGVTKVSYF AKENRTQIKA
     QYLRKLYLSM AKDIRVIIVK LADRLHNLKT IGYLKPERQQ IIARESLEIY SAIAHRLGMK
     AVKQEIEDIS FKIINPVQYN KIVSLLESSN KERENTINQK IEELKKILIT EKKMSVKVYG
     RSKSIYSIYR KMNQFGKNFD DIHDILAVRI ITNSVDDCYK VLGFVHQHYT PLNNRFKDYI
     ATPKHNLYQS LHTTIVADDG LIFEVQIRTE EMDELAEQGV AAHWRYKEGE NYDIAKKQKD
     IDERLDIFKR ILDLENISVQ ERDEIQQEVY KPDHLMEQII QNDIFSSLIY VLTPNGKVVT
     LPFGSTVLDF AYKIHSEIGE KTIGAKINGL FSPISTVLKS GDVVDIKTAA TQKPNHSWLV
     VSKTSSALEK IKKYLKKELV EVTSDAKSVN LEKIKQTKSQ IEEYIAKKDL KWKLVNSETQ
     LERLHAINFN NIEDFLLDVA NDEYTLEEAI NLVYLDHETS QNEKILKKLQ DKQYKKAQLK
     DDIIVQGISN IKVVISQCCL PIPYEDITGY VSKAEGIKVH LKTCRNIQSG DKQDRQVEVS
     WNEAVCKNKQ YDCAIRIEAI DRPALLVDVT KVLSHLNASV QMMSANVSGD LMNLTIKTII
     KVSNADRLQQ IRSSLLTIPD IKVVERVMM