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Database: UniProt
Entry: A0A1G9RBC4_9BURK
LinkDB: A0A1G9RBC4_9BURK
Original site: A0A1G9RBC4_9BURK 
ID   A0A1G9RBC4_9BURK        Unreviewed;       753 AA.
AC   A0A1G9RBC4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SDM20167.1};
GN   ORFNames=SAMN05428957_103138 {ECO:0000313|EMBL:SDM20167.1};
OS   Oryzisolibacter propanilivorax.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Oryzisolibacter.
OX   NCBI_TaxID=1527607 {ECO:0000313|EMBL:SDM20167.1, ECO:0000313|Proteomes:UP000198552};
RN   [1] {ECO:0000313|Proteomes:UP000198552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPL6 {ECO:0000313|Proteomes:UP000198552};
RA   Varghese N., Submissions S.;
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; FNHP01000003; SDM20167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9RBC4; -.
DR   STRING; 1527607.SAMN05428957_103138; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000198552; 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:SF36; 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:SDM20167.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198552};
KW   Transferase {ECO:0000313|EMBL:SDM20167.1}.
FT   DOMAIN          71..170
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          415..476
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          677..750
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   753 AA;  82999 MW;  CD9A04051B26D2AD CRC64;
     MAFPSSNAQA VTAAKPVDAA VAASNAAAAS FAALLEKLDY LTEAEAEQVR LAYRYADQAH
     LGQLRSSGEP YITHPIAVAA LCASWKLDAQ ALCAALLHDA MEDCGITKSD LVERFGTPVA
     ELVDGLTKLD KLQFNTREEN QAESFRKMLL AMARDVRVIL IKLADRTHNM RTLSDMPRSK
     WRRISSETLE VYAPIAHRLG LNQTYRELQD LSFRHLHPWR YETLSKAVAR SRNRSRDSVQ
     KMQSDVDAAF VRMGLPARVS GREKTLYAIY QKMTEQHLSF AQVIDLYGFR VVVASVLDCY
     TALGVLHQAF KPVPGRFKDH IAIAKLNGYQ SLHTTLVGPA GLNVEFQIRT EEMHIVAEAG
     VAAHWLYRAR AASGEVGESA EPMDTQWLQS LLDIQNETRD AAEFWDHVKV DLFPDAVYVF
     TPRSQILALP RGATVVDFAY AIHSDVGDRT VGARINNEQV PLRTELRNGD VVEVMTAQGA
     RPNPAWLGFV RTARARSKIR HYLKSLVQAE SAGLGEKLLA QALRAEGIQQ LPDAQEQSAL
     WDRLLHATGS RSQTELLTDI GLGRRIAGIV AKRLAGLLAE GGQRPDAVLL SRERYAGHEN
     LSQGAITVDG SESAPVQYAT CCRPVPGDPV VGYLGRGEGL VVHHAQCGVA QRLQRKDAER
     FIAVDWADEP ARLFDAGITV TVNNGKGVLA RIASELSNSE ADIVRMDMDD AMATTELRFV
     VAVRDLSHVE AVLRNLRRAP SVVRVWRVLP HAA
//
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