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Entry: A0A1G5EUU8_9PROT
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Original site: A0A1G5EUU8_9PROT 
ID   A0A1G5EUU8_9PROT        Unreviewed;       714 AA.
AC   A0A1G5EUU8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SCY30747.1};
GN   ORFNames=SAMN05216308_10787 {ECO:0000313|EMBL:SCY30747.1};
OS   Nitrosospira sp. Nsp13.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855332 {ECO:0000313|EMBL:SCY30747.1, ECO:0000313|Proteomes:UP000198731};
RN   [1] {ECO:0000313|EMBL:SCY30747.1, ECO:0000313|Proteomes:UP000198731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp13 {ECO:0000313|EMBL:SCY30747.1,
RC   ECO:0000313|Proteomes:UP000198731};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMVD01000007; SCY30747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5EUU8; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000198731; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase 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; 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;
KW   Kinase {ECO:0000313|EMBL:SCY30747.1};
KW   Transferase {ECO:0000313|EMBL:SCY30747.1}.
FT   DOMAIN          57..156
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          398..459
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          641..714
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   714 AA;  79547 MW;  A9CB3D1A73B93909 CRC64;
     MRARGLPDPS ATLPEADFLF GELSGYLKPE DISELQNAYL FSQSAHSGQF RKSGEPYISH
     PLAVAGILGK LRLDPQTLTA ALLHDVMEDT HVSKAEISDR FGKPVAELVD GVSKLDKIEF
     QTHADAQAEN FRKMLLAMAR DVRVILIKLA DRLHNMRTLE AMRPEKRRRI ARETMEIYAP
     IANRLGLNNI YQELQELSFR YLFPTRYRVL TNATKAARGN RREVVTKILD SIKQRLQAAG
     LDAEVTGREK QLYSIYKKMA EKHLTFSEVL DIYGFRVIVK DVPSCYIALG ALHSLYNPIP
     GKFKDYIAIP KANGYQSLHN TLWGPYGTPI EVQIRTADMH RIAEAGVASH WLYKSTDADL
     NDLHMKTHQW LQSLLETLSD STDSLEFLEH LKVDLFPGEV YVFTPQGKIL ALPKDATAVD
     FAYAVHTDIG DCCVAAKING ENAPLRTHLR SGDRVEIVTA SHAKPNPAWL NYVVTGKARS
     HIRRFLKTMQ YEESAKLGER LLNQALMSLK IDPQTISETQ WEKLARESSA KSKKDLLADM
     GLGMHLPAVI ARRLASPGES ASGANGGNGV ITILGTEGMA VQFAKCCRPI PGDPIVGFIK
     KDQGLVIHIH DCPVISKNRG NSDNWLDVAW GKGIARHFEV SIRTVVANQR GVLARVAAAI
     AEAGSNIDNV VMEGDGAYTT MNFMLQVRNR YHLAQVMRSL RRIPEVAKIT RMKG
//
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