ID A0A023X3P1_9ACTN Unreviewed; 744 AA.
AC A0A023X3P1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:AHY46615.1};
GN ORFNames=RradSPS_1332 {ECO:0000313|EMBL:AHY46615.1};
OS Rubrobacter radiotolerans.
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY46615.1, ECO:0000313|Proteomes:UP000025229};
RN [1] {ECO:0000313|EMBL:AHY46615.1, ECO:0000313|Proteomes:UP000025229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY46615.1,
RC ECO:0000313|Proteomes:UP000025229};
RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA da Costa M.M.S.;
RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT RSPS-4.";
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}.
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DR EMBL; CP007514; AHY46615.1; -; Genomic_DNA.
DR RefSeq; WP_038681550.1; NZ_CP007514.1.
DR AlphaFoldDB; A0A023X3P1; -.
DR STRING; 42256.RradSPS_1332; -.
DR KEGG; rrd:RradSPS_1332; -.
DR PATRIC; fig|42256.3.peg.1349; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000025229; Chromosome.
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:UP000025229};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 61..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 399..460
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 663..737
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 561..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 83263 MW; 5E7088B2E8DEE7D8 CRC64;
MDAARKDTEL RQVPEPEVTI SDLLAKVRAY CPEGAEAVVS EAYAVAHAAH RGQFRRSGEP
FVYHPLATAG ICADLRLDPT TVAAALLHDV IEDTGVTKEE LAERFGESLA EIVDGVTKLT
RLPSDSVEET QAESLRKMIV AMSRDVRVII IKLADRLHNM RTLAYLKRET QHKKATETLE
IYAPLAHRLG IYSVKWELED LAFATLHPRR YEEIKRLVDA RRADREAFIN ETGEKLKEQL
REAGVEAEVK GRVKHFYSIY NKMIRRNKEF NEIYDLAGLR VVVGSTRDCY GALGVIHSVW
KPMPGRFKDY IAMPKFNMYQ SLHTTVMSNE GKLLEIQIRT KEMDTTAEYG IAAHWMYKEG
GRDAEVDRLT WLKSMMEWQR EMTDAGEFMD SLKGELVADE VFVFTPKGKV ISLPAGATPI
DFAYHVHTEV GHKTIGAKVN GRIVPLDSEL VSGDRVEIIT GKNASPSRDW LTVVQSGRAR
NKIRQHYNRA DREDNASLGR EKVTALLKKR HARKVPHEVF EEVGREVGHN NADDLFAAVG
AGTVSTESVV GRVLDRIKPE EDEAEAKKVA SPAFSPLPLP EEEGRPDRET GVRVVGSSGI
MTRLARCCTP MPGDDIVGYV SLGRGVVVHD SGCANARALR ARDPERFVEV EWAAGNGKLF
TVELQVEALD RMNLLRDITT TISDAGVSIL SARVDTIENR TALSRFAFRA ASRQHVEEIV
RKVRSIPDVY DVYRVSRDGT PIDK
//
