ID A0A089MCD7_9BACL Unreviewed; 726 AA.
AC A0A089MCD7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=R70331_24220 {ECO:0000313|EMBL:AIQ54329.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ54329.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ54329.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ54329.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009284; AIQ54329.1; -; Genomic_DNA.
DR RefSeq; WP_042179633.1; NZ_CP009284.1.
DR AlphaFoldDB; A0A089MCD7; -.
DR STRING; 1536773.R70331_24220; -.
DR KEGG; paee:R70331_24220; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000029487; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000029487};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 44..143
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 384..445
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 652..726
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 549..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 479..506
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 82838 MW; 467D04EF9E33774A CRC64;
MGIEQLVEKA GAYIKEKDLL RIREAYEFAD QAHHGQVRKS GEPYILHPLA VADIVVNMQM
DVISIIAALL HDVVEDTTVS LEQIREKFGD TCAMLVDGLT KLERIRFRSK EEQQNENYRK
MFIAMAQDIR VIVIKLADRL HNMRTLKYQS EDSQRRISYE TLEIFCPIAD RLGISAIKWE
MEDIALRYLN PQQYYRIANL MHKKRAEREQ FIDSVIGRIR AKLDEMGIEG DLSGRPKHIY
SVYNKMSTKN KQFNEIYDLL AIRIIVDNIK DCYATLGIIH TLWKPMPGRF KDYIAMPKAN
MYQSLHTTVV GPGGEPTEVQ IRTWEMHRTA EFGIAAHWAY KEGSSNTGNP ENRMPFFREI
LELQHEAKDA EEFVESLKMD FFSDLVFVFT PKGEVVELPA GSVPLDFAFR IHTEVGNRTI
GSKVNGRIVP LDHKLKTGDI VEILTSKNSY GPSRDWLKIA QSSHARSKIK QWFKKEKREE
NVEKGREAVE RELKRLNMEV SDFLTEDKLS DVAKKFAFGD VEDMLSAVGF GGITASQIAN
KLTEKLRREQ EEAANHLELS TEMKEIKSSG GNRNQPTNGV RVKGIDNLLV RFARCCNPVP
GDDIVGYVTR GRGVSVHRED CPNIPTDGDG EESARVIEVE WEGSMEANYS VDIEITGHDR
NGLLNEVLQA VSESKTNISA VTGRSDKNKM AMIHMTILIR NTDHLQSVVD RVKRVKDVYT
VNRIMQ
//
