ID A0A1U7NLK9_9FIRM Unreviewed; 734 AA.
AC A0A1U7NLK9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=BO225_07925 {ECO:0000313|EMBL:OLU45675.1};
OS Dubosiella newyorkensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dubosiella.
OX NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU45675.1, ECO:0000313|Proteomes:UP000186705};
RN [1] {ECO:0000313|EMBL:OLU45675.1, ECO:0000313|Proteomes:UP000186705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU45675.1,
RC ECO:0000313|Proteomes:UP000186705};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-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:OLU45675.1}.
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DR EMBL; MPKA01000082; OLU45675.1; -; Genomic_DNA.
DR RefSeq; WP_076341729.1; NZ_MPKA01000082.1.
DR AlphaFoldDB; A0A1U7NLK9; -.
DR STRING; 1862672.BO225_07925; -.
DR GeneID; 78275864; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000186705; Unassembled WGS sequence.
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; 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; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000186705};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 391..460
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 659..734
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 734 AA; 83953 MW; 53871774F33A5D3D CRC64;
MSVKGEVTFE ECKENIKTYI KRPENLDLIQ RAYEFAHEHH KGQFRKSGAP YEVHVIQVAN
TLATLRCGPK TIAAGLLHDT VEDCEGVDHD VIAANFGEEI AVIVDAVTKI RAIKFKDEKE
YLASNHRKLF IALAKDIRVI LVKLADRLHN MRTLEFMPEA KQKKIASETL QVYAPIAHRL
GISQVKNELE DLSFKYLYPE KYEQIKRLVR QRESDRNEQV QEMIADIEKI LKMYSIPYRI
FGRSKHFYSI YKKMKTKNKR FEEILDLQAI RIVTDSEVHC YEILGYIHAK YRPIPGRFKD
YIAMPKANMY QSLHTTIVDP DTGHIFEIQI RTEQMDAVAE QGVAAHWKYK ERPGVNTEIE
QKEIEDKLSW FRDFSMMTDE ESEDPLEYMN VLQKDIFEAN VYCMSPRGKI IALPPGSTPI
DFAYRIHTEV GHKTVGATVN GAIVPLNTQL KTGDVVDILT SNHSNGPSKD WIKIVKSGHA
RNKIRAFLQK QEHQNRKELI KKGEADLAEE FKRLKIDDSK RSVKRLESIL QTLSFKTVDD
LYIGIANRRV SLQSVVDRLV KRNGNVSDDE IVKIFNKNNE KSAKTNSCGV IVPGIETIAV
SLANCCSPIP QDTIVGYISK GQGVKVHRSD CPNIAHETKR LIPVQWVEDQ DDTKVYEVKL
VVFSDDRNYL LSDIVTILQQ SKAYLKHVDS AVDDNLLTAT TKLTIGVHNA DHLQTVISNL
KKVRSVNEVQ RTIQ
//
