ID V6Q3F3_9ENTE Unreviewed; 738 AA.
AC V6Q3F3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=T233_01740 {ECO:0000313|EMBL:EST89292.1};
OS Vagococcus lutrae LBD1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST89292.1, ECO:0000313|Proteomes:UP000018126};
RN [1] {ECO:0000313|EMBL:EST89292.1, ECO:0000313|Proteomes:UP000018126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBD1 {ECO:0000313|EMBL:EST89292.1,
RC ECO:0000313|Proteomes:UP000018126};
RX PubMed=24371201;
RA Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA Earl A.M., Gilmore M.S.;
RT "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT Isolated from the Largemouth Bass Micropterus salmoides.";
RL Genome Announc. 1:e01087-13(2013).
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:EST89292.1}.
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DR EMBL; AYSH01000020; EST89292.1; -; Genomic_DNA.
DR RefSeq; WP_023607044.1; NZ_AYSH01000020.1.
DR AlphaFoldDB; V6Q3F3; -.
DR STRING; 1408226.T233_01740; -.
DR PATRIC; fig|1408226.3.peg.1702; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000018126; Unassembled WGS sequence.
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:EST89292.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000018126};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EST89292.1}.
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..738
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 84462 MW; DE5C2560412819C4 CRC64;
MPKEEVLSSE DVIRLVSGYM GEEHVAFVRR ACAFAEKAHE GQVRKSGEIY FMHPIQVAGI
LAELRMDPYT VATGFLHDVV EDTPVTKEDI AAEFGETVAM LVDGVTKLGK IKYKSHEEQL
AENHRKMLLA MAQDLRVIMV KLADRLHNMR TLKHLRADKQ RRIAKETLEI YAPLAHRLGI
SRIKWELEDT ALRYLNPQQY YRIVHLMNSK RDEREAYIDR TVEDIRVATE ELDIYAQIYG
RPKHIYSIYR KMKDQKKEFE EIYDLLAIRV LVDTIKDCYA VLGAIHTKWK PMPGRFKDYI
AMPKTNMYQS LHTTVIGPNG NPVEVQIRTH EMHEVAEFGV AAHWAYKEGK TDGVAETEES
RQLSWFHDII ELQDESHDAS DFMESVKGDI FSDKVYVFTP KGDVTELPKG SGPLDFAYNI
HTEIGNKTTG AKINGKMVPL DYKLKNGDII EVLTSANSFG PSRDWLQLVA TSRARNKIRR
FFKDQDRELN IAKGKESLEK QLIAMDFSPK EMMSKARMTE FLSKQNYHNE EDLYAVIGNG
EITAQTIANR LTESERRERE KIRKQQEADE LLQQPMKKDS EKIKVRHEGG IVIQGVENLL
IRISRCCNPV PGDDIVGYIT KGRGVSIHRQ DCPNIVNNDE ASQRLIEVEW EDTAASSDQE
YNADLEIYGY NRSGLLNDVL LVVNGMTKNL ISVEARPGRN KTATIHLTLS IQNLSHLKQI
VDKIKTIPDV YSVRRTNG
//
