ID A0A2S0ME21_9BURK Unreviewed; 737 AA.
AC A0A2S0ME21;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AVO34142.1};
GN ORFNames=C6570_07725 {ECO:0000313|EMBL:AVO34142.1};
OS Ottowia oryzae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=2109914 {ECO:0000313|EMBL:AVO34142.1, ECO:0000313|Proteomes:UP000239709};
RN [1] {ECO:0000313|EMBL:AVO34142.1, ECO:0000313|Proteomes:UP000239709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KADR8-3 {ECO:0000313|EMBL:AVO34142.1,
RC ECO:0000313|Proteomes:UP000239709};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Ottowia sp.";
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; CP027666; AVO34142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0ME21; -.
DR KEGG; otk:C6570_07725; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000239709; Chromosome.
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; 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; 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; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:AVO34142.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239709};
KW Transferase {ECO:0000313|EMBL:AVO34142.1}.
FT DOMAIN 409..470
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 666..737
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 737 AA; 81122 MW; 4569E59BAF3474FB CRC64;
MKSMPLRPPA AGAPAADVVT ATSAGVQDES GVRARARAFA VPLLAGETSS AGESLMEHAD
AVADILLTIG GSESLQAAAY LSYASAQLNR PDEVIGKAFD DGLARLAIET SKLERVQKRS
RAMRDDQASD SELASQQTEY VRKMLLAFSR DLRVVLLRLA SRLQTLRYGA AKRKPLAPML
LRESHEVFAP LANRLGIWQI KWEMEDLIFR AQEPDTYKLV ASLLDEKRAE REAALEQRRA
DIEAALCAQG IQAQVSGRPK HISSIVRKMR GKGLDFDQVF DVRALRVLVP SVDECYAALG
WVHQHFTPVP DEFDDYIAKP KINGYQSLHT VVRDADHRAW EIQIRTPQMH EHAEHGVAAH
WAYKEAGTKG YVGVTAASDY DAKIAVLRQL LAWERDLSGT GPQYGLFDDR IYVLTPDAAI
VELPAGATPV DFAYTVHTEL GHRCRGAKVD GALVQLNTPL KNGQTVEVVV AKDGGPSRDW
LNPDLGYLAS SRARAKVRAW FNAQQTRETT ARGRDMVEKL LQREGKTSVS KDFLAAELGY
KNPDALFETV GKDELSLRSI ETVLRPPAPQ PDADAQVLLK KPRPEGGTRG GVLVVGMDSL
LTQPARCCKP APPDPIGGYV TRGRGVTVHR RDCASFRDLL AREPERVIDV EWSTPATGRS
AAYPVDVAVE ATDRQGLLRD ISDVFTREKM NVIGVQTQSV KGWAWMTFTV EVSDTQRLSQ
VLREVLAVPG VRVAKRR
//
