ID   A0A1B3PNB1_9BURK        Unreviewed;       761 AA.
AC   A0A1B3PNB1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:AOG24250.1};
GN   ORFNames=BSY15_616 {ECO:0000313|EMBL:AOG24250.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG24250.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP016447; AOG24250.1; -; Genomic_DNA.
DR   RefSeq; WP_069103554.1; NZ_CP016447.1.
DR   AlphaFoldDB; A0A1B3PNB1; -.
DR   STRING; 1842533.BSY15_616; -.
DR   KEGG; acra:BSY15_616; -.
DR   PATRIC; fig|1842533.3.peg.652; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000094760; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094760}.
FT   DOMAIN          80..179
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          421..482
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          684..759
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  84146 MW;  E37AB722C80A2120 CRC64;
     MNAVLISPSA TPPRPGESAA PASGSLSAAA AAANAAAASF AALTDSLDYL DAASIEQVRQ
     AYRFADEAHL GQLRSSGEPY ITHPIAVAAQ CATWKLDAQA LMAALLHDAM EDCGVTKADL
     IDRFGLPVAE LVDGLTKLDK LQFNTREENQ AESFRKMLLA MARDVRVILI KLADRTHNMR
     TLSDMPRSKW GRISSETLEI YAPIAHRLGL NQTYRELQDL AFRHLHPWRY ATLYKAVNKS
     RNRRRDLVQK VQAEVDAAFS KIGMKVRLAG REKTLYAIYQ KMDHKHLSFA QVTDIYGFRV
     IVPTVTDCYT AMGVLHQMYK PVPGKFKDHI AIAKLNGYQS LHTTLVGPSG VNIEFQMRTD
     EMHVIAEAGV AAHWLYKAQD ADGTSAERLG TKWLQSLLDI QNETRDAAEF WDHVKVDLFP
     DAVYVFTPKS QIMALPRGAT VVDFAYAIHS NVGDRTTAAK INNEQVPLRT ELKNGDVVEV
     ITAPVSAPNP AWLGFVRTGR ARSKIRHYLK TLAQAESEGL GEKLLTQAIR AEGMEQLPPV
     NAETQPMWEK LLRFTGNRTR SELMTDLGLG KRIASIVAKR LMVLMAEHGH RPNALLLSKE
     RYTSHETLSQ GAVTLDGSEN ASVQYASCCR PVPGDSIVGY LGRGEGLVVH NTHCGVAKRL
     QHKDSERFIA VDWSDEPTRM FETGIVVTVN NGKGVLARIA AELANAEADI THVDMDDEVA
     LDTIDLRFIV AVRDQNHLET ALRNLRRTAA VIRAMRLTPQ A
//