ID A0A091C162_9ENTE Unreviewed; 737 AA.
AC A0A091C162;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=TMU3MR103_1825 {ECO:0000313|EMBL:KFN89792.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN89792.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN89792.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN89792.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) 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}.
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:KFN89792.1}.
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DR EMBL; JPVT01000195; KFN89792.1; -; Genomic_DNA.
DR RefSeq; WP_038024017.1; NZ_JPVT01000195.1.
DR AlphaFoldDB; A0A091C162; -.
DR PATRIC; fig|1302648.3.peg.1786; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000029381; 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:KFN89792.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381};
KW Transferase {ECO:0000313|EMBL:KFN89792.1}.
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 663..737
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 551..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 84636 MW; CB0550117CC0766B CRC64;
MAKDSVISGP SVIKLVSYYM SNEHTAIVEH AYEYAAEAHK EQYRKSGELY IVHPVQVAGI
LAELHMDPHT IAAGFLHDVI EDTEVTLEDL ETEFGSDVAM IVDGVTKLGK IKYKSHEEQL
AENHRKMLLA MAQDLRVIMV KLADRLHNMR TLKHLRDDKQ RRIARETLEI YVPLADRLGI
SRIKWELEDL SLRYLNPKQY YRIVHLMQSK RDQREKYVSQ AVEEIRVATE ELNIYAEIYG
RPKHIYSVYR KMVDKKKQFD EIYDLLAIRV IVDSIKDCYA VLGAIHTKWK PLPGRFKDYI
AMPKANMYQS IHTTVIGPHG SPVEVQIRTH QMHEIAEFGV AAHWAYKEGH TEKIQPDELT
GQVGWFKELL ELQDESFDAS DFMESVKGDI FSDKVYVFTP KGDVSELPKG SVPLDFAYHI
HTDIGNKTVG AKINGKMAQL DYKLRNEDIV EVLTSPNSFG PSRDWLKFVA TSKARNKIKR
FFKAQDREEN IEKGHGMLVK TLQEMDFSAK EVLIKTKIQD VLERFNFHTE DDLYAAVGYG
EISATTLANR LTEEQRRKRQ EEKEKQRVQD MVNSSNKKEP EKMKIRHDGG VIIQGVQNLL
VRISHCCNPV PGDEIVGYIT KGRGVSIHRK DCPNIENSPE MENRLIEVEW EDTSNTNKEY
NAEVEVNGYD RSGLLNEILQ AVSSQNDRIV NVEAHSNKEK TATIRITVSI KNLSHLQSIV
DKIKQVPDIY SVHRLKG
//
