ID A0A0G1X500_9BACT Unreviewed; 472 AA.
AC A0A0G1X500;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KKW26061.1};
GN ORFNames=UY68_C0001G0054 {ECO:0000313|EMBL:KKW26061.1};
OS Parcubacteria group bacterium GW2011_GWF2_52_12.
OC Bacteria.
OX NCBI_TaxID=1618976 {ECO:0000313|EMBL:KKW26061.1, ECO:0000313|Proteomes:UP000034153};
RN [1] {ECO:0000313|EMBL:KKW26061.1, ECO:0000313|Proteomes:UP000034153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKW26061.1}.
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DR EMBL; LCQX01000001; KKW26061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1X500; -.
DR PATRIC; fig|1618976.3.peg.60; -.
DR Proteomes; UP000034153; 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; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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; 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; PF13328; HD_4; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KKW26061.1};
KW Transferase {ECO:0000313|EMBL:KKW26061.1}.
FT DOMAIN 42..140
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 377..438
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 472 AA; 54091 MW; 0E71391AFB1F04A2 CRC64;
MEPLTNIVNS LNSLPDRELV SRAYVFAREA HEGQLRYSGE PYITHPLAVA GILTEQHADA
KTIAAGLLHD CLEENHGVRE CLKKEFGPEI FFLVEGVTRL GHLKYKGAER HAESLRKLFI
ATAKDIRVLL IRLADRLHNV RTLAAVPEEK RLRIAVETIE IYAPLANRLG MGQLKEELED
GAFPFTLPEE HTLVKKLLKE KRRETQPRLE KMYRALARSL AVAGMKNFSI DYRAKGLYSL
YKKLLRYKMD IEKVYDLIAL RVIVESISDC YQALGIVHML WKPAPERIKD YIATPKPNGY
QSIHTSVFVG DGTVAEVQIR TADMHREAEY GVSSHMAYKE RNMSKRLAWI DELLKLQREY
KENEEFLENL KMDFFQDRIF VFTPKGDVVE LPEGASVLDF AFCIHSDIGM HASAATVSGK
YSPLDYKLKS GDIVKIETKK TSRPSHKWLD YVKTSMARKH IRMSLMPKKE ED
//
