ID   I3Z5J9_BELBD            Unreviewed;       741 AA.
AC   I3Z5J9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:AFL84517.1};
GN   OrderedLocusNames=Belba_1936 {ECO:0000313|EMBL:AFL84517.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL84517.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) 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; CP003281; AFL84517.1; -; Genomic_DNA.
DR   RefSeq; WP_014772496.1; NC_018010.1.
DR   AlphaFoldDB; I3Z5J9; -.
DR   STRING; 866536.Belba_1936; -.
DR   KEGG; bbd:Belba_1936; -.
DR   PATRIC; fig|866536.3.peg.1991; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_2_10; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000006050; Chromosome.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   CDD; cd04876; ACT_RelA-SpoT; 1.
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; 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; 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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006050}.
FT   DOMAIN          405..466
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   741 AA;  84887 MW;  42A89694152A7DC1 CRC64;
     MIQVDLEEER KEILKRYRKL LKLAKPLLKD SDAKVIKKAF NVSNEAHKEM RRKSGEPYIY
     HPLEVALVCV EEIGLGPTSI VAALLHDVVE DTDWELEDIE REFGHKVMQI IDGLTKISGV
     FDYGSSQQAE NFRKMLLTLS DDVRVILIKI ADRLNNMRTL SSMPRHKQLK IASETMYLYA
     PLAHRLGLYT IKSELEDLYL KYTDTDTYNF IVEKINETRL SRNKFIKSFI APLEEELTEQ
     GFNFTIKGRP KSVYSIYNKM KKQNIPFEEV YDLFAVRIIV NTEEDNEKAD CWQVYSVVTD
     FYRPNPDRLR DWISTPRSNG YESLHTTVMS NTGQWVEVQI RSQRMDDIAE RGYAAHWKYK
     DRAAAATKAS TGLDDWITQV RTLLESNDGS AIEFMDDFRG NLFHDEVFVF TPKGDLKVMP
     IGATALDFAF EIHTEVGAKC IGAKVNQKLV SINHKLKNGD QVEILTSSKQ KPTEDWLNQV
     VTSRAKAKIK DALREEKKSS ILDGREIVQR KLKQMKLDFN SETVEQLRAY FETKTANEFY
     YKVGKGIIES TSIKGFKDFK EEKRQKGKAS FEVVKDESSF TKEIKNLKGP DHDQLLIGED
     MDLVDYVLAK CCNPIPGDDV FGFVTINEGI KIHRTSCPNA LELLSNHGNR VIKAKWTSQQ
     EIAFLAGLRI VGTDRVGLIN DVTKVISNEL KVNMRSITVD SDAGIFEGTI KLYVHSTQHL
     EKLMDNLAQV EGIIKITRFD Y
//