ID A0A3P1WNN7_9ACTN Unreviewed; 751 AA.
AC A0A3P1WNN7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RRD47941.1};
GN ORFNames=EII42_01460 {ECO:0000313|EMBL:RRD47941.1};
OS Tessaracoccus sp. OH4464_COT-324.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD47941.1, ECO:0000313|Proteomes:UP000274803};
RN [1] {ECO:0000313|EMBL:RRD47941.1, ECO:0000313|Proteomes:UP000274803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD47941.1,
RC ECO:0000313|Proteomes:UP000274803};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD47941.1}.
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DR EMBL; RQYZ01000001; RRD47941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1WNN7; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000274803; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:RRD47941.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000274803};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 74..171
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 677..751
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 751 AA; 83989 MW; ED1763549707D4F0 CRC64;
MESRENADSQ LPWQRVRHRL ARIGAPRPRS AVLDPLFSIV RANHPKADLE VISRAYRTAE
QHHAGQFRQR GEPYITHPLA VATILAELGM TEPVIVAALL HDTVEDTDYT LEQCQADFSE
EVAKMVDGVT KLDKLTYGDT AKAETIRKMI VATSEEVRVL VIKLADRLHN MRTLGTLRPD
KRIRIATETL NIFAPLAHRL GMNTIKWELE DLSFQVIEPQ FYNEIVDMVQ QAAPEREATL
RALISQFQKM LSEAKITATV YGRPKHYYSI YQKMMVRGRD FRDIYDLIGL RVLVDEPKDC
YTVLGVAHAA WKPIPGRFKD YIANPKFNLY QSLHTTVLGA NQEPVELQIR THEMHRRAEY
GVAAHWKYKQ NLRNGITPEE AGLRAMHQLA VMSKETEDPS EFLDSVLFEI NSDEIFVFTP
KGEVTALPAG ATPVDFAFSV HTEVGYRCIG ARVNGRLVSL STPLQQGDKV EILTAKTEDA
GPSRDWLSFV VSSRAKQKIR QHFSRERRDE AIEQGKELLA KELRRAGVPL QRLLNLENLT
AVANELGQKN VSCLYSAVGE GHLGPQHVIG KLIALHGGED EALDTVSEDQ PSVEGRKKTR
QAATAVVLVD GDDAVVAKFA KCCSPLPGDE IIGFVTKGDG VSVHLRSCSN VPALLEQPER
IVDVRWNANT GEAFLVTLEL LGMDRSGLLS DVTAVLAQQH VDIVSVNINS NKQRQFTGRV
TFEAADPTHL QHIINQVRRV PGVFDVYRVQ G
//
