ID A0A087DGG6_9BIFI Unreviewed; 776 AA.
AC A0A087DGG6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:KFI94616.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:KFI94616.1};
GN ORFNames=BSTEL_1286 {ECO:0000313|EMBL:KFI94616.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI94616.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFI94616.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI94616.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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}.
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:KFI94616.1}.
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; JGZP01000021; KFI94616.1; -; Genomic_DNA.
DR RefSeq; WP_034530004.1; NZ_JGZP01000021.1.
DR AlphaFoldDB; A0A087DGG6; -.
DR STRING; 762211.BSTEL_1286; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000029004; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000029004};
KW Transferase {ECO:0000313|EMBL:KFI94616.1}.
FT DOMAIN 67..164
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 423..486
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 689..763
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 366..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 86490 MW; 5A6C1CE4E732E0E0 CRC64;
MAGDDMEFDS ARKLGCEVST DPINPLLPIM QACRVHHPGE DLTILERAYR RAVIQHSAQR
RKSGEPYIIH PLAVAQILAD LGMGPLVVAA GLLHDTVEDT DYTLDQCRAE FGDTVTGLVD
GVTKLSKMEY GDSAQAETIR KMVVAMSRDV RVLVVKLADR VHNARTWRYV KTSSAVKKAH
ETLDVYAPLA NRLGMNAIKT ELEELSFKVI YPKIYNEIVV LVARRAGQRD VYLKQILAEI
NEDLDAQHIK AYVTGRPKDY FSIYQKMIVR GHDFANIYDL VGVRIIVDSI QDCYAALGAV
HARWNPVPGR FKDYIAMPKL NMYQSLHTTV VGPGGKPVEI QIRTWDMHRR AEFGIAAHWK
YKENGQAGRA LSSPDKSDRK REGSENQELS EADNLKWIQQ LADWTSETPD SNEFLGSLKE
DLGSAEVYVF TPKGKIISLP AAATPIDFAY AVHTEVGHRT MGARVNGRLV PLDTKLENGD
TVEILTSKSD TAGPSRDWLS FAKSPKARNK IRQWFSKERR SEAIEEGRDE LTRAMRKRSL
PINTLLTPEA LIGVADELNF PNADGLFAAI GDGQISTQNV ISHLVKDAGA DEVDEEIEQE
VLPLKPVETR QKTNSSSGVS VKGVGDVWVK LARCCMPVPG DKIIGFITRN QGVSVHRTDC
QNMIDLQRRQ PERVVEVEWT STKGVFMVKI QVEALDRRNL LSDVTRVLSD HGVNIISGSI
STGSDRVATS QFSFEMADPQ HLNTLLAAVR KIEGVFDVYR ITGAKDSAEP RLRRMQ
//
