GenomeNet

Database: UniProt
Entry: A0A329KM59_9BACL
LinkDB: A0A329KM59_9BACL
Original site: A0A329KM59_9BACL 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system