ID A0A0U5B7W8_9BACL Unreviewed; 729 AA.
AC A0A0U5B7W8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN Name=relA {ECO:0000313|EMBL:BAU27036.1};
GN ORFNames=CB4_01205 {ECO:0000313|EMBL:BAU27036.1}, DFP93_104120
GN {ECO:0000313|EMBL:PYE62473.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU27036.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU27036.1, ECO:0000313|Proteomes:UP000217696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU27036.1,
RC ECO:0000313|Proteomes:UP000217696};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PYE62473.1, ECO:0000313|Proteomes:UP000247363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8566 {ECO:0000313|EMBL:PYE62473.1,
RC ECO:0000313|Proteomes:UP000247363};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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}.
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DR EMBL; AP017312; BAU27036.1; -; Genomic_DNA.
DR EMBL; QJSZ01000004; PYE62473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5B7W8; -.
DR KEGG; asoc:CB4_01205; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000217696; Chromosome.
DR Proteomes; UP000247363; 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:BAU27036.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000217696};
KW Transferase {ECO:0000313|EMBL:BAU27036.1}.
FT DOMAIN 52..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 654..728
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 729 AA; 83444 MW; 126391784B8094CD CRC64;
MSIETAIETA IDQVTDKAKT YLPQKDIEFL IRAYEFAREA HEGQIRKSGQ PYIIHPIAVA
GILIDLQMDA VTVAAAFLHD VVEDTEVTSE QIAENFGQEV ANLVEGVTKL GRIKLKSKAQ
QQAENHRKMF LAMAKDLRVV MIKLADRLHN MRTLKYLPEP KQRQISDETL EIFAPLAHRL
GIASIKWEME DTGLRYINPQ QYYRIVNLMK KKRAEREKYI HGVIDLLQER LKELSITSEI
SGRPKHIYSI YRKMVKQNKE FNEIYDLLAV RIIVDDIRDC YAALGIVHTL WKPMPGRFKD
YIAMPKANMY QSLHTTVIGP NGEPLEVQIR TAEMHRIAEY GIAAHWAYKE GQNISEEATF
ETKLSWFREI LEWQQEARDA QEFMESLKMD LFADLVFVFT PKGDVIELPK GSVPLDFAYR
IHSEVGNRTI GSKVNGKIVP LDHQLKTGDI IEILTSKHSY GPSRDWLKIT KSTQARSKIK
QWFKREKREE NVMKGREMVE AELKRNSFEP KEIMTAENLL EVANKFNFQG EEDMFAAVGY
GGITGAQIAT RLTDKLRKER EDMMPNTAEI RTDAPRKRPD NGVSVRGIDN LLIRFSRCCN
PVPGDDIVGF ITRGRGVSVH RGDCPNLQSC SEDDQARLIS VEWDADMKHE FNVDIEVTGH
DRSGLLNEVL ATVADMKTNI TAVSGKTDKN RVAKINMTIA IQNLDHLHKV VERIKKIRDV
YSVRRVLNT
//
