ID E4SIE0_LACAR Unreviewed; 746 AA.
AC E4SIE0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN OrderedLocusNames=LA2_04865 {ECO:0000313|EMBL:ADQ58939.1};
OS Lactobacillus amylovorus (strain GRL 1112).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=695560 {ECO:0000313|EMBL:ADQ58939.1, ECO:0000313|Proteomes:UP000007033};
RN [1] {ECO:0000313|EMBL:ADQ58939.1, ECO:0000313|Proteomes:UP000007033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRL 1112 {ECO:0000313|EMBL:ADQ58939.1,
RC ECO:0000313|Proteomes:UP000007033};
RX PubMed=21131492; DOI=10.1128/JB.01365-10;
RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RT "Genome sequence of Lactobacillus amylovorus GRL1112.";
RL J. Bacteriol. 193:789-790(2011).
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}.
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DR EMBL; CP002338; ADQ58939.1; -; Genomic_DNA.
DR RefSeq; WP_013437743.1; NC_014724.1.
DR AlphaFoldDB; E4SIE0; -.
DR GeneID; 66523721; -.
DR KEGG; lam:LA2_04865; -.
DR PATRIC; fig|695560.3.peg.972; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000007033; Chromosome.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
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 672..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 746 AA; 85307 MW; 99096F4E97A64E75 CRC64;
MSKYVEMTHD QVIDACKKYM NDKQVAFVEK AYEFANKAHA GQKRASGQPY IIHPTQVAGT
LATLGLDPDT VAAGFLHDTV EDTPVTNDEL KEKFGEDVAF IVDGVTKLNK YEYKSHQEFL
AENHRKMLIA MAKDLRVIMV KLADRLHNMH TLQHLRPDKQ RRIASETMDI YAPLADRLGI
GTIKWELEDM SFHYLNPEAY YRIVNLMDVK RSQREKYIAD TIKTLKKTLD ELGIKYEIYG
RPKHIYSIYK KMVNKHKDFD EIYDLLAVRV IVKNVRDCYA VLGAVHTEWK PMPGRFKDYI
AMPKVNGYQS LHTTIIGPGG RPLEIQIRTE AMHQVAEYGV AAHWAYKRGN FNGVEATSSG
EKLDMVREIL ELKDETKDAG EFMKSVKSDI FSDRVYVFTP KGEVYELPKG SVTLDFAYAI
HTQVGSHAVG AKVNNKLVPL DYKLRNGDVI EIMTQTNATP SRDWADMVKT SRARNKIRRY
FRGQDREESI NHGEQMVANM IREEGLAPKD FMDKEHIERL LDHFNYHTEE ELYAAVGFGD
LSAQAVVNRL TVDLRREDEK QKQKELEEKI LNSGQQSVQE EQPKKNSNSV MKVKHKNGVM
IQGVSDLMLH LAKCCNPVPG DKIIGYVTKG RGVTIHRTDC RNITKEAEEQ GRLIDVEWEN
VEENSVQSFN ANIEIFGYNR SNLLSDVINK LNSLTKNINN ISGKVNEDNI AHIYVTVAVK
NANQLDEILS KLRDIPDVYE TKRSDN
//
