ID   H5Y8M7_9BRAD            Unreviewed;       761 AA.
AC   H5Y8M7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN   ORFNames=Bra471DRAFT_04610 {ECO:0000313|EMBL:EHR03819.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR03819.1};
RN   [1] {ECO:0000313|EMBL:EHR03819.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR03819.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) 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; CM001442; EHR03819.1; -; Genomic_DNA.
DR   RefSeq; WP_007611189.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5Y8M7; -.
DR   HOGENOM; CLU_012300_3_0_5; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000005774; 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; 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; 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; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
FT   DOMAIN          80..179
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          424..485
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          687..761
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   761 AA;  85152 MW;  C0D651B8D8D8E5F8 CRC64;
     MVYRRRTPTQ MQAATESVAV APTAPVARPA KPRARMMRQY DLVERVRSYN PNTDEDLLNR
     AYVYAMKAHG SQTRASGDPY FSHPLEVAAI LTDLKLDDAT IVAALLHDTI EDTEATRAEI
     DQIFGPEIGA LVEGLTKLKR LELVSREAKQ AENLRKLLLA IADDVRVLLV KLADRLHNMR
     TLDFVPTESR RRIAEETLDI YAPLAGRMGM QEMREELEDL SFRTLDPEAY SVVMQRLDAL
     AERNRNLIGE IEDQLSNNLR HRGLGARVYG RRKKPFSIWT KMERKSVGFE QLSDIFGFRV
     VVNDIEACYR ALGIVHTNWP VVPGRFKDYI STPKQNDYRS IHTTVIGPGN QRVELQIRTE
     AMDQIAERGI AAHVFYKEGV GSPTEFLKRE SNAFAWLRHT IGILSESANP EEFLEHTKLE
     LFHDQVFCFT PKGKLIALPR HANVIDFAYA VHTDVGNSAV GCKINGQFAP LSSELQNGDE
     VEVLTSEAQA APPSAWETLA VTGKARAAIR RATRTAVRDQ YVGLGRRIVE RLFERAKIEY
     ADDKLKGALP RLARTSIEDV MAAVGRGEIK ASHVARAMYP DYKEERIARY GVKKGLAAKL
     KEKSSEPPRS PVAIPIRGIN SDLPVKFAPN GGAVPGDRIV GIVTPGEGIT IYPIQAPALK
     DFEEEPERWL DVRWDIEDSA PQRFPARIKV ENVNEPGALA QIATVIAEHD GNIDNISMQR
     RSPDFTETTI DLEVYDLKHL SAILAQLRAK AVVARAERVN G
//