ID A0A1Q8E6T6_9STRE Unreviewed; 733 AA.
AC A0A1Q8E6T6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BU202_07545 {ECO:0000313|EMBL:OLF47503.1};
OS Streptococcus cuniculi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1432788 {ECO:0000313|EMBL:OLF47503.1, ECO:0000313|Proteomes:UP000186890};
RN [1] {ECO:0000313|EMBL:OLF47503.1, ECO:0000313|Proteomes:UP000186890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NED12-00049-6B {ECO:0000313|EMBL:OLF47503.1,
RC ECO:0000313|Proteomes:UP000186890};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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:OLF47503.1}.
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DR EMBL; MSJM01000006; OLF47503.1; -; Genomic_DNA.
DR RefSeq; WP_075105179.1; NZ_MSJM01000006.1.
DR AlphaFoldDB; A0A1Q8E6T6; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000186890; 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: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:OLF47503.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OLF47503.1}.
FT DOMAIN 49..148
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 387..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 658..733
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 733 AA; 83221 MW; 2FC0E247E53D2252 CRC64;
MKEINLTGED VIALTAQYMP EEDVAFVRKA LEYAVEAHSQ QFRKSGEPYI IHPIQVAGIL
AGLQLDAVTV ACGFLHDVVE DTDVTLDEME AEFGSDVRMI VDGVTKLGKV EYKSHEEQLA
ENHRKMLIAM SKDMRVILVK LADRLHNMRT LKHLRKDKQE RISRETMEIY APLAHRLGIS
SIKWELEDMA FRYLNETEFY KITHLMTEKR REREALVNEV VDKIREFASE HHLHGHIYGR
PKHIYSIYRK MHDKKKRFDQ LYDLIAIRCI METPSDVYAM LGYIHELWRP MPGRFKDYIA
NPKANGYQSI HTTVYGPKGP IEFQIRTAEM HQVAEYGVAA HWAYKRGGKA TASQQELKWI
NNLIELQADA GDAQTFVDSV KDDIFTERIY VFTPDGSVRE LPKDSVPIDF AYEIHTKVGE
KATGAKVNGR MVPLTTKLKT GDQVEIITSA NSFGPSRDWI NLVKTHKARN KIRQFFKNQD
KELSITKGRE LIQNLLQENG YVANQYLDRK HLDDVLQKTS YKTDEALFAA VGFGEISAMS
IFNRLTEKER REAERAKAKA VADELVNGGE VKQDNKDSLK IRHEGGVVIE GASGLLIRLA
KCCNPVPGDA ITGYITKGRG VAVHRADCMN LKSQENYEVR LIDVSWEDEP SSKEYMANID
IYGLNRSGLL NDVLKVLTNS SKNISSVNAQ PTKDMKFATI HVSFGIPNLA TLTSVVDKIK
SVPEVYSVKR TNG
//
