ID G5KDS7_9STRE Unreviewed; 739 AA.
AC G5KDS7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=STRUR_1945 {ECO:0000313|EMBL:EHJ56880.1};
OS Streptococcus urinalis 2285-97.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ56880.1, ECO:0000313|Proteomes:UP000005388};
RN [1] {ECO:0000313|EMBL:EHJ56880.1, ECO:0000313|Proteomes:UP000005388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ56880.1};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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:EHJ56880.1}.
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DR EMBL; AEUZ02000001; EHJ56880.1; -; Genomic_DNA.
DR RefSeq; WP_006739619.1; NZ_AEUZ02000001.1.
DR AlphaFoldDB; G5KDS7; -.
DR STRING; 764291.STRUR_1945; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000005388; 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: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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000005388};
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 664..739
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 739 AA; 84026 MW; E16DDE364801F4C4 CRC64;
MAKEVNLTGD EVLDLTKKYM NESDVAFVKK ALDYATAAHF YQARKSGEPY IIHPIQVAGI
LADLHLDAVT VACGFLHDVV EDTDITLDDI ELDFGKDVRD IVDGVTKLGK VEYKSHEEQL
AENHRKMLMA MSKDIRVILV KLADRLHNMR TLKHLRKDKQ ERISRETMEI YAPLAHRLGI
SRIKWELEDL AFRYLNEVEF YKISHLMSEK RREREALVDE IVEKITTYTN EQGLYGEVYG
RPKHIYSIYR KMRDKKKRFD QIFDLIAIRC IMETASDVYA MVGYIHELWR PMPGRFKDYI
AAPKANGYQS IHTTVYGPKG PIEIQIRTKD MHAVAEYGVA AHWAYKKGIK GKVNQAEQKV
GMNWINELVE LQDASNGDAK DFVDSVKEEI FSERIYVFTP NGAVQELPKD SGPIDFAYAI
HTQVGEKATG AKVNGRMVPL TAKLKTGDVV EIVTNPNSFG PSRDWIKLVK TNKARNKIRQ
FFKNQDKEMS INKGRELLVD YFQEQGFVAN KYLEKKRIDE ILPRLSVKSE EALYAAVGFG
DLSPVSVFNK LTEKERREEE RAKAKAEAEE LLHGGEIKHE NREVLKVKSE NGVIIQGASG
LLMRIAKCCN PVPGDPIEGY ITKGRGIAIH RADCNNIKSQ EGYEQRLIEV EWDEANSSKE
YQAEIDIYGL NRSGLLNDIL QILSNATKSI SSVNAQPTKD MKFANIHVSF GIPNLAHLTT
VVDKIKIIPD VYSVKRTNG
//
