ID A0A1L8RGI3_9ENTE Unreviewed; 737 AA.
AC A0A1L8RGI3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=RU97_GL001494 {ECO:0000313|EMBL:OJG18876.1};
OS Enterococcus canis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=214095 {ECO:0000313|EMBL:OJG18876.1, ECO:0000313|Proteomes:UP000181884};
RN [1] {ECO:0000313|EMBL:OJG18876.1, ECO:0000313|Proteomes:UP000181884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17029 {ECO:0000313|EMBL:OJG18876.1,
RC ECO:0000313|Proteomes:UP000181884};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-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:OJG18876.1}.
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DR EMBL; JXKH01000003; OJG18876.1; -; Genomic_DNA.
DR RefSeq; WP_067394268.1; NZ_JXKH01000003.1.
DR AlphaFoldDB; A0A1L8RGI3; -.
DR STRING; 214095.RU97_GL001494; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000181884; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000181884};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
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 552..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 84302 MW; EC5583F32B965C3B CRC64;
MAKDEIMTGP GVIKMVSRYM SPEHTAFVEK ALEYATKAHE GQTRKSGEPY IIHPIQVAGI
LAELHMDPQT VATGFLHDVV EDTEVTLEDL REEFGESVAM LVDGVTKLGK IHYKSHEEQL
AENHRKMLLA MAQDLRVIMV KLADRLHNMR TLKHLREDKQ RRIAQETLEI YAPLAHRLGI
SRIKWELEDT ALRYLNPKQY YRIVHLMQSK REEREAYVAE AVEDIRQATE ELSIYAEIYG
RPKHIYSIYR KMKDQKKQFD EIYDLLAIRV IVDSIKDCYA VLGAIHTKWT PMPGRFKDYI
AMPKANMYQS LHTTVIGPKG NPVEVQIRTH EMHQIAEFGV AAHWAYKEGR TEKVSADAST
NQLSWFREIL ELQDESYDAS EFMESVKGDI FSDKVYVFTP KGDVTELPKG SGPLDFAYSI
HTEIGNKTTG AKVNGKMVQL DYKLKNGDII EVLTSPNSFG PSRDWLNMVA TSKARNKIKR
FFKVQDREMN ISKGQEAVAK QLSEHQFSPK EFMSKAKVSE VLDRFNFQSE DDMYAAVGYG
ELSAQMLANR LTEKERRQQE QERQKQEADE LMSQPVKKEP EKMKVRHEGG IVIQGVDNLL
IRISRCCNPV PGDPIVGYIT KGRGISIHRA DCPNVQNKDE IAERLIEVEW EDTSNTKKEY
AADLEIYGYN RSGLLNDVLQ TISNMTKNLV SVDAKPAKNK MAIIHLTVSI QNLPHLERIV
DKIKSVPDVY SVRRTKG
//
