ID A0A3D9RY26_9BACL Unreviewed; 728 AA.
AC A0A3D9RY26;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=A8990_11513 {ECO:0000313|EMBL:REE84338.1};
OS Paenibacillus taihuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1156355 {ECO:0000313|EMBL:REE84338.1, ECO:0000313|Proteomes:UP000256304};
RN [1] {ECO:0000313|EMBL:REE84338.1, ECO:0000313|Proteomes:UP000256304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10966 {ECO:0000313|EMBL:REE84338.1,
RC ECO:0000313|Proteomes:UP000256304};
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 (AUG-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}.
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:REE84338.1}.
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DR EMBL; QTTN01000015; REE84338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9RY26; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000256304; 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:REE84338.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:REE84338.1}.
FT DOMAIN 44..143
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 654..728
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 728 AA; 82947 MW; F2B286518B40A199 CRC64;
MGIEQLLDKA STYLKEQDLT RIKEAYEFAD QAHHGQVRKS GEPYILHPVA VAEILVNMQM
DVLSIIAALL HDVVEDTTVP LEEVRSRFGD ACAAVVDGLT KLEKIKFRSK EEQQNENYRK
MFVAMAQDMR VILIKLADRL HNMRTLKYQS EEAQRRVAYE TLEIFCPIAH RLGMSAIKWE
MEDIALRYLN PQQYYRIANL MKKKRAEREQ YITDVISRIR EKLEDMGIEG DISGRPKHIY
SIYKKMTARS KQFNEIYDLL AIRIIVDNIK DCYATLGIIH TLWKPMPGRF KDYIAMPKAN
MYQSLHTTVI GPTGEPTEVQ IRTWDMHRTS EFGIAAHWAY KEGGVVPAGS FEDKMTLFRE
IIELQHEASD ASEFVESLKM DFFSDLVFVF TPKGEVFELP AGAVPLDFAY RVHTEVGNRT
IGSKVNGRIV PLDYKLKTGD IVEILTSKHS YGPSQDWIKI AQSSHARSKI KQWFKKEKRE
ENVIKGRDSI ERELKRLGLE PSSFMSDPQL QEAALKFTFN DIDDMLSAVG FGGITAAQIC
TKLTERMRRE AEEASQIELT NEMKEVKSSP AHQRKSRPTH GVVVKGVDNL LVRFARCCNP
VPGDIIVGYI TRGRGVSVHR ADCLNLTSSA EGEEAARMIE VEWEESVEAN YSVDIEITGH
DRPGLLNEVL QAVSESKTNI SAVSGRSDKN KLAMIHMTVL IKNIEHLGSV VERIKRVKDI
YSVQRIMQ
//
