ID   Q47N46_THEFY            Unreviewed;       814 AA.
AC   Q47N46;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   01-MAY-2013, entry version 59.
DE   SubName: Full=RelA/SpoT protein;
DE            EC=2.7.6.5;
GN   OrderedLocusNames=Tfu_2090;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5-'
CC       diphosphate) is a mediator of the stringent response that
CC       coordinates a variety of cellular activities in response to
CC       changes in nutritional abundance (By similarity).
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
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DR   EMBL; CP000088; AAZ56123.1; -; Genomic_DNA.
DR   RefSeq; YP_290146.1; NC_007333.1.
DR   ProteinModelPortal; Q47N46; -.
DR   STRING; 269800.Tfu_2090; -.
DR   EnsemblBacteria; AAZ56123; AAZ56123; Tfu_2090.
DR   GeneID; 3579350; -.
DR   KEGG; tfu:Tfu_2090; -.
DR   PATRIC; 23904826; VBITheFus33945_2246.
DR   eggNOG; COG0317; -.
DR   HOGENOM; HOG000018301; -.
DR   KO; K00951; -.
DR   OMA; VEDTGYS; -.
DR   ProtClustDB; CLSK2769477; -.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:EC.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR026020; (p)ppGpp_Synthase.
DR   InterPro; IPR012675; Beta-grasp_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   PANTHER; PTHR21262; PTHR21262; 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; SSF81271; TGS-like; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Transferase.
SQ   SEQUENCE   814 AA;  91379 MW;  2CA2D3A8EB31EDD3 CRC64;
     MRSETVSTHT KPVRPEPPAP AAEVPAGAFP PGQERDHDTR PSAPPRDQSP PPAPEADSRS
     AARPAPPTHP GTSSTVWVRR RLARLGAQRG TTMNPVLEPL VKTVRATHPK ADIRLIERAY
     DVAAHYHRSQ KRKSGDPYIT HPLAVATILA ELGMQEATIA AGLLHDTVED TEYTLDQLRS
     DFGDEIAELV DGVTKLDKVK YGEATQAETV RKMVVAMARD IRVLVIKLCD RLHNMRTLRY
     LPQAKREKKA RETLEIYAPL AHRLGMNTIK WELEDLAFAT LYPKRFDEIA RLVAERAPRR
     DVYLQEVIEI VSADLREAKI KATVRGRPKH YYSIYQKMIA RNVGFDEIYD LVGIRVIVDS
     VRDCYAALGI IHARWNPVPG RFKDYIAMPK FNMYQSLHTT VIGPEGSPVE LQIRTRAMHR
     RAEYGIAAHW KYKEERNNGG KAKGASTDMA WLRQLIDWQQ ETKDPGEFLE SLRFDLSVQE
     VFVFTPRGDV IALPQGATPV DFAYAVHTEV GHRTVGARVN GRLVPLDSEL HNGETVEIIT
     AKTDDAGPSR DWLDFVKSAR ARNKIRQWFT KERREAAIEQ GKEAIAKVMR KQELPVQRLF
     TSESLIALAH DLRYRDLDAL YAAVGENQIS AHKVVEKLIE SVGSLDNNEE DIAEATTPIR
     VPRKRPTGNP GVVVQGDPDV WVRLSKCCTP VPGDAIIGFV TRGAGVSVHR DDCGNVKHLD
     PDRLVQVEWQ PTGNSMFLVA LQIEALDRTR LLSDITRVLS DQHVNILSAT VQTTRDRVAL
     SRFTFEMADP AHLGHVLKAV RSVDGVYDVY RVRN
//