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Database: UniProt
Entry: J1ED57_9BURK
LinkDB: J1ED57_9BURK
Original site: J1ED57_9BURK 
ID   J1ED57_9BURK            Unreviewed;       742 AA.
AC   J1ED57;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:EJE50199.1};
GN   ORFNames=PMI14_05285 {ECO:0000313|EMBL:EJE50199.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE50199.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE50199.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE50199.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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   -!- 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:EJE50199.1}.
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DR   EMBL; AKJX01000198; EJE50199.1; -; Genomic_DNA.
DR   RefSeq; WP_007858348.1; NZ_AKJX01000198.1.
DR   AlphaFoldDB; J1ED57; -.
DR   PATRIC; fig|1144317.3.peg.4832; -.
DR   Proteomes; UP000004811; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   CDD; cd04876; ACT_RelA-SpoT; 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; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
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; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT   DOMAIN          409..470
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          671..742
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   742 AA;  81552 MW;  F5301CEF491BD9C7 CRC64;
     MKTLAPPPGP PLNTAEAVPQ LIAATAHTLP EQVNALVRAR AFAEPLIASE ALDSGENTLA
     HADAVAAILK SIGGSEAMQA ASYLVYSCVH LNKPEEVITK AFGANFAALA VETTKLVRVQ
     QQARGAQALD DPALQTENVR KMLLAFSRDL RVVMLRLASR LQTLRFHAAT KLPMSPSLAR
     ESLQVFAQLA NRLGIWQVKW ELEDLSFRFL EPDTYKEVAR LLDEKRGERE VYMEQLRARL
     ESDLRARSIS ASVQGRPKHI YSIVKKMRGK SLNFDQVYDI RALRVVVPTV KDCYAALSWV
     HQRFAPIVEE FDDYIAKPKA NGYQSLHTIV RDDLNGKPIE IQIRTQAMHE HAEHGVAAHW
     AYKEAGAKGY VGVSATGEYD AKIAVLRQLL AWERDLAGHA QKSNGLFEDR IYVLTPEAAV
     VDLPQGATPV DFAYSVHTSL GHRCRGAKVD GVMVPLNTPL QNGQTVEIVT VKEGRPSRDW
     LNAELGYLTS NRAKAKVRAW FNAQATHETV ARGREAVERL LQREGKTAVK LDDLAVQLGF
     KSAEALFEVV GKDEFSLRNI ETVLRPAEPP PSSDDYLLLK KPRGNESSGP KGGVLVVGID
     SLMTQLAKCC KPAPPDDIRG FVTRGKGVSV HRSDCSNFRE MAARNGERVI DVDWGLPKAS
     AADKPAVYPV DVAVEAADRQ GLLRDISEVF AREKTNVIGV QTQSVKGTAW MTFTVEVADS
     GRLNKVLGIV AGVQGVRSAR RR
//
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