ID A0A3P5XWQ8_9BACL Unreviewed; 732 AA.
AC A0A3P5XWQ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN Name=relA {ECO:0000313|EMBL:VDC32581.1};
GN ORFNames=FILTAD_02789 {ECO:0000313|EMBL:VDC32581.1};
OS Filibacter tadaridae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Filibacter.
OX NCBI_TaxID=2483811 {ECO:0000313|EMBL:VDC32581.1, ECO:0000313|Proteomes:UP000270468};
RN [1] {ECO:0000313|EMBL:VDC32581.1, ECO:0000313|Proteomes:UP000270468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATB-66 {ECO:0000313|EMBL:VDC32581.1};
RA Criscuolo A.;
RL Submitted (NOV-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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; UXAV01000044; VDC32581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P5XWQ8; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000270468; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:VDC32581.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000270468};
KW Transferase {ECO:0000313|EMBL:VDC32581.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 658..732
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 732 AA; 83640 MW; 0654FCB65E0AF81C CRC64;
MAKNRDMTAE DIFARVGSYM NEEHVAFVVK AYEAAKNSHE GQFRSSGEAY IIHPIQVAGI
LAELEMDPST MAAGFLHDVV EDTAVSREDI IRDFGEEVAM LVDGVTKLDK LKYKSKEEKQ
AENHRKMFIA MAQDIRVILI KLADRLHNMR TLKHVSEEKQ RRISAETLEI FAPLAHRLGI
SAIKWELEDI ALRYLNPQQY YRIVNLMKRK RVERENYLEK VMTEIKEEIS DMDIVADISG
RPKHLYSIYR KMVLQKKEFN EIYDLLAVRI LVPSIKDCYA VLGSIHTLWK PMPGRFKDYI
AMPKQNFYQS LHTTVVGPAG DPLEVQIRTE EMHKIAEFGV AAHWAYKEGK KLTGDSKDID
SKLTWFREIL EIQNESSNAE EFMESLKFDL FSDMVYVFTP DGDVMELPDG SVPIDFAYRV
HSEVGNRTIG AKVNGKMVPL DTELHTGDII EILTSKQSFG PSRDWLKIAN TSQAKNKIRQ
FFKKQLREEN IIKGREMIEK EVKAQEFDLK DVLTQGNTKR VIEKFSFTSE EDMYAAVGFN
GITAQQVVNR LAEKLRKERE QLDTINKIVS DMNTAPPDKM TESGVIVRGI DNLLIRLSKC
CNPVPGDEIV GFITKGRGVS VHRSDCPNIS AGDEEIDRII EVEWAHGTSS TRKEFQVDIE
VSAFDRQGLL NEVMMVVAET KTTMVAVSGK ADRDKIARIN MTIKITDIAH LHRIVDRIKQ
VRDIYSVQRV IN
//
