ID A0A1L8MKY0_9STRE Unreviewed; 739 AA.
AC A0A1L8MKY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=A9Q68_09305 {ECO:0000313|EMBL:OJF71371.1};
OS Streptococcus bovimastitidis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1856638 {ECO:0000313|EMBL:OJF71371.1, ECO:0000313|Proteomes:UP000182015};
RN [1] {ECO:0000313|EMBL:OJF71371.1, ECO:0000313|Proteomes:UP000182015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ1587 {ECO:0000313|EMBL:OJF71371.1,
RC ECO:0000313|Proteomes:UP000182015};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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:OJF71371.1}.
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DR EMBL; LZDD01000003; OJF71371.1; -; Genomic_DNA.
DR RefSeq; WP_071794434.1; NZ_LZDD01000003.1.
DR AlphaFoldDB; A0A1L8MKY0; -.
DR STRING; 1856638.A9Q68_09305; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000182015; 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:OJF71371.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OJF71371.1}.
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 664..739
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 739 AA; 84036 MW; 04B3A0102C7D6356 CRC64;
MAKEINLSGE EVVALAANYM TKKDVAFVQK ALDYATEAHF YQARKSGEPY IIHPIQVAGI
LADLHLDAVT VTCGFLHDVV EDTDITIDDI EKEFGSDVKD IVDGVTKLGK VEYKSHEEQL
AENHRKMLMA MSKDIRVILV KLADRLHNMR TLKHLRKDKQ ERISRETMEI YAPLAHRLGI
SRIKWELEDL AFRYLNESEF YKISHMMREK RREREALVDE IVDKIITYTN DQGLYGDVYG
RPKHIYSIHR KMRDKKKRFD QIFDLIAIRC IMETQSDVYA MVGYIHELWR PMPGRFKDYI
AAPKANGYQS IHTTVYGPKG PIEIQIRTKE MHQVAEYGVA AHWAYKKGIK GKVSQSDQKV
GMNWINELVE LQDASNGDAK DFVNSVKEEI FSERIYVFTP NGAVQELPKE SGPIDFAYAI
HTQVGEKATG AKVNGKMVPL TAKLKTGDVV EIVTNPNSFG PSRDWINLVK TNKARNKIRQ
FFKNQDKELS VNKGRELLVN YFQEQGYVAN KYLEKKKIEE ILPRLSVKSV ESLYAAVGFG
DMSPVSVFNK LTEKERREEE RAKAKAEAEE LVKGGEVKHE NKEVLKVRSE NGVIIQGASG
LLMRIAKCCN PVPGDAIDGY ITKGRGIAIH RTDCNNIKSQ EGYEQRLIEV EWDMENSSKD
YQAEIDIYGL NRSGLLNDVL QILSNSTKSI SAVNAQPTKD MKFANIHVSF GIPNLTHLTT
VVEKIKAVPD IYNVKRTNG
//
