ID F9P7T2_STRCV Unreviewed; 738 AA.
AC F9P7T2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=ANG5_1768 {ECO:0000313|EMBL:GAD45240.1}, HMPREF1042_1945
GN {ECO:0000313|EMBL:EGV08307.1};
OS Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1035184 {ECO:0000313|EMBL:EGV08307.1, ECO:0000313|Proteomes:UP000003287};
RN [1] {ECO:0000313|EMBL:EGV08307.1, ECO:0000313|Proteomes:UP000003287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1060 {ECO:0000313|EMBL:EGV08307.1,
RC ECO:0000313|Proteomes:UP000003287};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAD45240.1, ECO:0000313|Proteomes:UP000016985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 46377 {ECO:0000313|EMBL:GAD45240.1}, and CCUG46377
RC {ECO:0000313|Proteomes:UP000016985};
RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA Shintani S.;
RT "Genome Sequences of seven clinical isolates and type strains of anginosus
RT group streptococci.";
RL Submitted (SEP-2013) 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; AFUP01000004; EGV08307.1; -; Genomic_DNA.
DR EMBL; BASX01000017; GAD45240.1; -; Genomic_DNA.
DR RefSeq; WP_006268267.1; NZ_BASX01000017.1.
DR AlphaFoldDB; F9P7T2; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000003287; Unassembled WGS sequence.
DR Proteomes; UP000016985; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000313|EMBL:GAD45240.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 392..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 663..738
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 84358 MW; BFF96D4E26CFFF2B CRC64;
MPKEVNLTGD QVVALTRKYL SSEDVTLIQK ALFYAVDRHR GQFRQSGEPY IIHPIQVAGI
LAKLKLDAVS VACGFLHDVV EDTAATLDDL EGEFGHDVRV IVDGVTKLGK VKYMSHEEQL
AENHRKMLMA MSKDIRVILV KLADRLHNMR TLKHLRKDKQ ERISRETMEI YAPLAHRLGI
SSVKWELEDL AFRYLNPTEF YKISHLMKEK RREREDLVDE VVHKIETYAS ERNLHGQIYG
RPKHIYSIYR KMQDKKKRFD EIYDLIAIRC ILDTQSDVYA MLGYIHELWR PMPGRFKDYI
ANRKANGYQS IHTTIYGPKG PIEFQIRTKE MHEVAEYGVA AHWAYKKGIK GQVDSKESAI
GMNWIKEMME LQDQSNDAQD FVDSVKENYL AEEIYVFTPD GAVRSLPKDS GPIDFAYEIH
TKVGEKAVGA KVNGRMVPLT TKLKTGDQVE IITSSNSFGP SRDWINLVKT SKARNKIRQF
FKNQDKELSI CKGRELLQAQ FQENGYVANK YMDKRHMEEV LQKTSYKTEE TLFAAIGFGE
VSAVSIFNRL TERERREEER AKARAEAEEL VKGGEVKVEN KDTLKVKHEG GVIIQGASGL
LIRIAKCCNP VPGDEIVGYI TKGRGVAIHR KDCMNLRAQE NYEQRLIDVE WEDNSSVKEY
TAHIDIYGLN RTGLLNDVLQ VLSNTTKNIS TVNAQPTKDM KFANIHVSFG IANLSMLTTV
VDKIKSVPEV YSVKRTNG
//
