ID D2BLW9_LACLK Unreviewed; 740 AA.
AC D2BLW9;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA {ECO:0000313|EMBL:ADA63920.1};
GN OrderedLocusNames=LLKF_0073 {ECO:0000313|EMBL:ADA63920.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA63920.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ADA63920.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ADA63920.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
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; CP001834; ADA63920.1; -; Genomic_DNA.
DR RefSeq; WP_003132277.1; NC_013656.1.
DR AlphaFoldDB; D2BLW9; -.
DR GeneID; 69712154; -.
DR KEGG; llk:LLKF_0073; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000001886; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000313|EMBL:ADA63920.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADA63920.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000313|EMBL:ADA63920.1}.
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 665..740
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 549..579
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 740 AA; 83818 MW; 96B2F4CDC0569152 CRC64;
MPKEPDLTGA EVVNICSDYM NETDLLLVEK ALACASLAHA DQYRASGEAY FVHPTQVAGI
LAKLKLDAVT VSCGFLHDVV EDTNFTQGDL QELFGDEIAE IVDGVTKLGK VEYKSHEEQL
AENHRKMLMA MSKDIRVILV KLADRLHNMR TLKHLRPDKQ KRISRETMEI YAPLAHRLGI
ASIKWELEDL SFRYLEEAEF YRIRGLMNEK RTAREALVAE VIGKLQERVE KAGVDAEIYG
RPKHIYSIYR KMHDKKKRFD EIYDLIAIRC ITETTSDVYT TLGYIHDLWK PMPGRFKDYI
ANPKANGYQS VHTTVYGPKG PMEFQIRTRE MHQIAEFGVA AHWAYKQGIK AKVDVHEISE
TLNWIHELVE LREEAGDSAE DFVKAVQEDI LSDKIYVFTP NGEVQELPRG SGPIDFAYAI
HTKVGDHATG AKVNGRMKPL SVQLKTGDRV EIITSSSSFG PSRDWINLVK TNKARNKIKQ
FFKNQDKELS VNKGREMLQE ALEEGGFVPN QYLDKKHLDE VFNKISYRNA EALYAAIGFG
ELSATTIANR LTENERREVE RAKQKAEAEE LMKGEVKRES SKNIMKIRHD GGVSVSGIDS
LLVRIAKCCN PVPGDPIVGY ITKGRGVSVH RADCQNVRSM EDFEQRLVEV EWDDSENLVK
EYVANIDVYG FNRPGLLNDV MQVLSNSTKN LISINAQPTK DKKMANIHIA LGIKNLSDLT
LIVDKIKMTP DVYSVKRTNA
//
