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Database: UniProt
Entry: A0A2R8BYE3_9RHOB
LinkDB: A0A2R8BYE3_9RHOB
Original site: A0A2R8BYE3_9RHOB 
ID   A0A2R8BYE3_9RHOB        Unreviewed;       713 AA.
AC   A0A2R8BYE3;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   Name=rsh {ECO:0000313|EMBL:SPJ25195.1};
GN   ORFNames=PAA8504_03044 {ECO:0000313|EMBL:SPJ25195.1};
OS   Palleronia abyssalis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Palleronia.
OX   NCBI_TaxID=1501240 {ECO:0000313|EMBL:SPJ25195.1, ECO:0000313|Proteomes:UP000244912};
RN   [1] {ECO:0000313|EMBL:SPJ25195.1, ECO:0000313|Proteomes:UP000244912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8504 {ECO:0000313|EMBL:SPJ25195.1,
RC   ECO:0000313|Proteomes:UP000244912};
RA   Keele B.F.;
RL   Submitted (MAR-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; ONZF01000007; SPJ25195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8BYE3; -.
DR   Proteomes; UP000244912; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 2.
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   Kinase {ECO:0000313|EMBL:SPJ25195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244912};
KW   Transferase {ECO:0000313|EMBL:SPJ25195.1}.
FT   DOMAIN          52..151
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          389..454
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          634..708
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   713 AA;  80225 MW;  62D439AC0AB9CBE7 CRC64;
     MDDGAIWLED AERLIARVRS YNPRADIDRI RRAYAYGAAM HEGQFRHSGE PYITHPLAVA
     MILAEQQLDD ATLITALLHD TIEDTKSTFG DVADQFGFEI AELVDGVTKL TKLQLTSTET
     KQAENFRKLF MAMSRDMRVI LVKLADRLHN MRTIKAMRPD KQAQKARETM DIYAPLAGRM
     GMQWMREELE DHAFSVLNPE GRRSIIHRFA TLRREAGDVV DKITRDIRIE LDKAGIKGEV
     YGRAKRPFSI WRKMEEKNVG FSRLSDIYGF RVVVASEAEC YSVMGAIHQR WRAVPGRFKD
     YISQPKSNGY RSIHTTVSGR DAKRVEVQIR TRAMHEVAET GVAAHWSYRD GERVENPFAV
     DPATWVRALT EQFDAADDHA EFLEAVKLEM YSDQVFCFTP KGEVVKLPKG ATPLDFAYAI
     HTRIGERAVG AKVDTVRVPL WQKLRNGQSV EILTAEGQTP QASWLDLVTT GRAKSAIRKS
     LREADRDRFV RLGTELMRVA FDHVEKRMTD KAIGIAARAL GVPSGEELLA RVGSAELETR
     QVIAALFPGV TPRPADEIDA RSAVVGLEPN QPFGRARCCQ PLPGERIVGI SYRGEGVQIH
     AIDCEALAQV EDQPERWIDL AWQSGNHPAV HAVTFDMTIS NDAGVLGRIC TLIGSQKANI
     SDLKFLERRQ DFYQVLIDVD LRSIEHFHAV RMALEAEANV AMIERVRDPA LSP
//
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