ID A0A401HXW3_9BACL Unreviewed; 728 AA.
AC A0A401HXW3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=PA598K_02200 {ECO:0000313|EMBL:GBF73876.1};
OS Paenibacillus sp. 598K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF73876.1, ECO:0000313|Proteomes:UP000288287};
RN [1] {ECO:0000313|EMBL:GBF73876.1, ECO:0000313|Proteomes:UP000288287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=598K {ECO:0000313|EMBL:GBF73876.1,
RC ECO:0000313|Proteomes:UP000288287};
RA Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA Kimura A., Kitamura S., Hara H., Funane K.;
RT "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT an ability of degrading cycloisomaltooligosaccharides.";
RL Submitted (MAR-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:GBF73876.1}.
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DR EMBL; BFBX01000031; GBF73876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401HXW3; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000288287; 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; 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:UP000288287};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
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"
FT COILED 540..567
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 728 AA; 83336 MW; 71F37BC2B5EB9198 CRC64;
MGIEQLLEKA SAYLKEHDLQ SIREAYDFAE QAHHGQVRKS GEPYILHPVA VADIIVNMRM
DVISIIAALL HDVVEDTTVA LDEVRSRFGE TCAMLVDGLT KLEKIRFRSK EEQQNENYRK
MFVAMAQDIR VILIKLADRL HNMRTLKFQS EESQRRIAYE TLEIFCPIAH RLGMSAIKWE
MEDIALRYLN PQQYYRIANL MKKKRTEREN YIAEVVHDIT EKLEEMGISG DISGRPKHIY
SIYKKMTDKN KQFNEIYDLL AIRIIVDNIK DCYATLGIIH TLWRPMPGRF KDYIAMPKAN
MYQSLHTTVI GPNGEPTEVQ IRTWEMHRTS EYGIAAHWAY KEGSSTPEAS LGDKVSWFRE
ILELQHETSD AAEFMESLKM DFFSDLVFVF SPKGEVFELP AGSVPLDFAY RVHTEVGNRT
IGAKVNGRIV PLDYKLKTGD IVEILTSKHS YGPSQDWVKI AQSSHARSKI KQWFKKERRE
ENVAKGRELL ERELKRLGLE PSDWMSDNKL QEVAEKFTFN EYEDMLSAIG FGGITAAQIC
TRLTEKLRKE NEEANQIELT AEVKEVKAGG STEKKRPTHG VRVKGVDNVL VRFARCCNPV
PGDAIIGYIT RGRGVSVHRL DCPNVHASEE QGDEAARVIE VEWEDAVEAN YSVDIEITGH
DRRGLLNEVL QSVSESKTNI AAVSGRSDKN KLALIHMTIL IRNIEHLHAV VEKIKRVKDV
YSVQRIMQ
//
