ID A0A329KM59_9BACL Unreviewed; 731 AA.
AC A0A329KM59;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DQG13_26395 {ECO:0000313|EMBL:RAU93066.1};
OS Paenibacillus sp. YN15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1742774 {ECO:0000313|EMBL:RAU93066.1, ECO:0000313|Proteomes:UP000251619};
RN [1] {ECO:0000313|EMBL:RAU93066.1, ECO:0000313|Proteomes:UP000251619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN15 {ECO:0000313|EMBL:RAU93066.1,
RC ECO:0000313|Proteomes:UP000251619};
RA Niu L.;
RT "Paenibacillus sp.YN15.";
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}.
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:RAU93066.1}.
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DR EMBL; QMFA01000048; RAU93066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329KM59; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000251619; 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: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; GTP PYROPHOSPHOKINASE; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000251619}.
FT DOMAIN 44..143
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 388..449
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 656..730
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 546..573
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 731 AA; 83294 MW; 269CE96C5A496780 CRC64;
MSIEQLLEKA SAYMKESDLK RIREAYEFAE RAHSGQLRKS GEPYILHPLA VADILIGMNM
DTTSIIAALL HDVVEDTTVS LDVVEQQFGH TCAMLVDGLT KLERIKFKTK EEQQNENYRK
MFVAMAQDIR VILIKLADRL HNMRTLKFQS EESQRRIADE TLEIFCPIAH RLGISAIKWE
MEDIALRYLN PQQYYRIVNL MQKKRAEREQ YIADVIQRIN EKVSEMGIDS DISGRPKHIY
SIYNKMTVKN KQFSEIYDLL AIRVIVDNIK DCYAVLGIIH TLYKPMPGRF KDYIAMPKAN
MYQSLHTTVI GPNGEPLEVQ IRTWEMHKTA EFGIAAHWAY KENGSQPVTA SFGTGNKMNM
FSDILELQQE ARDASEFMES LKVDFFSDLV FVFTPKGEVI ELPAGSVPLD FAYRIHTEVG
NRTIGAKVNG RIVPLDHRLK TGDIVEILTS KHSYGPSQDW LKLAQSSHTK SKIKQFFKKE
KREENVEKGR DAIEREIRRI GFEPSQVMAD DKMLEVAAKF NFHDIDDMLS AVGFGGITAS
QICTRLTEKL RREKEQEETQ RQLEEAAKEI KTAPPEKKGR PTHGVRVIGV DNVLVRFARC
CNPVPGDSII GYITRGRGVS VHRTDCANIP AGDGEEGNRV IEVEWVDSVE ANYSVDIEIT
GHDRRGLLNE VLQVVSESKT IISAVSGRSD KNKMALIQMT ILIRNIDHLQ SVVDKIKRLK
DVYSVQRIMQ S
//