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Database: UniProt
Entry: R7IK92_9BURK
LinkDB: R7IK92_9BURK
Original site: R7IK92_9BURK 
ID   R7IK92_9BURK            Unreviewed;       710 AA.
AC   R7IK92;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=(P)ppGpp synthetase I {ECO:0000313|EMBL:CDE52179.1};
GN   ORFNames=BN620_02142 {ECO:0000313|EMBL:CDE52179.1};
OS   Sutterella sp. CAG:351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=1262975 {ECO:0000313|EMBL:CDE52179.1, ECO:0000313|Proteomes:UP000018107};
RN   [1] {ECO:0000313|EMBL:CDE52179.1, ECO:0000313|Proteomes:UP000018107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:351 {ECO:0000313|Proteomes:UP000018107};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CDE52179.1}.
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DR   EMBL; CBJA010000374; CDE52179.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7IK92; -.
DR   STRING; 1262975.BN620_02142; -.
DR   Proteomes; UP000018107; 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;
FT   DOMAIN          382..443
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          639..710
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   710 AA;  79822 MW;  73B1E6A462832751 CRC64;
     MAPDNKKTEA PVKVNWQLAR SMVEPLYAGQ CLETGEPRMS HVDGMASILR GIRDDDELIA
     AAYLSSVQDY LKNPEEWIEK SFGSKVLELC TDLQRLMKLS EQARSSNKEA NAASQPEKLR
     KMLLAMCGDL RVVLLRLASR LQTLRWFVMH PSDDAKIYAA ETLQLYSPLA NRLGIWQMKW
     ELEDLSLRFT RPEVYQEIVR HLDASRAERL AFVQQAVTKI RSLLAAHHIR GEVSGRSKHI
     YSIWLKMERK HLPFERLFDL RALRVIVDTV EQCYEVLSIL NENFTAIQSE YDDYIAHPKP
     NGYRSLHTVV KASNGLPVEI QIRTREMHEF AELGFAAHWR YKEAGNSLGV NSAEEQKVVW
     LRQLLAWHSD VEPPRAPGVE DDLIYALTPM GRVVELAANS TPVDFAYMVH TQLGHRCRGA
     KVNGAIVPLT HKLKTGDTVE IIAAKSGGPS QDWMNPELGF AAMARTRGKV RTWFNQLHLQ
     EQIARGRDEL DTELARLGKS TYNLESLAKT LGFESVDDLC LTIAKDEISN RAIEAVVLPQ
     TQKKAADEPV IPVKPAQPRA HHDNGQILVA GVGSLLTQLA KCCHPVPPDE IVGFVSRGRG
     VVVHRADCPN VKNLMEQSKE RLIEVSWGDA PEDTLYPMEI LVLARDRIGL LKDVTDVFIR
     LKINITNVNT QTVKNVARLK FGVEVAGAAL MRQALKEILE VKGVISAHRS
//
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