ID   A0A2S0P7R4_9NEIS        Unreviewed;       718 AA.
AC   A0A2S0P7R4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:AVY93365.1};
GN   ORFNames=DAI18_04375 {ECO:0000313|EMBL:AVY93365.1};
OS   Microvirgula aerodenitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Microvirgula.
OX   NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY93365.1, ECO:0000313|Proteomes:UP000244173};
RN   [1] {ECO:0000313|EMBL:AVY93365.1, ECO:0000313|Proteomes:UP000244173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BE2.4 {ECO:0000313|EMBL:AVY93365.1,
RC   ECO:0000313|Proteomes:UP000244173};
RA   Anderson E., Jang J., Ishii S.;
RT   "Denitrifier Microvirgula.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP028519; AVY93365.1; -; Genomic_DNA.
DR   RefSeq; WP_028498088.1; NZ_CP028519.1.
DR   AlphaFoldDB; A0A2S0P7R4; -.
DR   STRING; 1122240.GCA_000620105_00616; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000244173; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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:AVY93365.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244173}.
FT   DOMAIN          60..159
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          401..462
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          644..718
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   718 AA;  79703 MW;  3EEACEA8E6C4C9C2 CRC64;
     MNSADAHTID YDAMVNAQAE ALLSTAATYL KPDDVPFLRT AFEFARDAHT GQTRKSGEPY
     ITHPLAVAQI LTEWKLDAQG LAAALLHDTM EDTGVAKATL AERFGKQVAE LVDGLSKLER
     LEYQSKESRQ AENFRKMVLA MARDIRVIII KLADRLHNMR TLDSMREEKR RRIAQETLDV
     YTPIANRIGL NKVYRELEDL CFKHLYPNRY HVLSKAVKAA RGNRRELVGK IMQSLARKLL
     EANIEATIRG REKNLYSIYH KMQEKHLSFS EVLDIYAFRV IVNDVPGCYL ALGALHGLYK
     PIPGKFKDYI AIPKSNGYQS LHTTLFGPYG TPIEVQVRTR EMHKIAETGV ASHWMYKSGG
     PTMDAARQRT HQWLQDILDI QAETGDAVEF YEHIKIDLFP DEVYVFTPKG KILVLPQGAT
     PVDFAYAVHT DIGHRCIAAK VNHELVPLRT ELKNGDTVEV ITAAHSKPNP SWLNFVVSGR
     ARSAIRSYLK TLHREEARVL GDRLLKQSIH SLAAQPFVLS DGVWSAYLKE VGDKNVKSTD
     VLASIGAGKQ QAMVVAARLL ELAGEVLGGP ARSGPLVIRG NEGSSIQYAA CCSPLPGERI
     AAALTKGQGM VLHTRDCAQL KRLDPDRVLD AEWEIRTPRL FSVPVTILAQ SARGALASVA
     AAISEGGANI ESVDMQDAHH GEGYVQIHFR LQVGSAQHLN EVLNHILAQP LVERAVRG
//