ID   D1AEV7_THECD            Unreviewed;       807 AA.
AC   D1AEV7;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   29-MAY-2013, entry version 30.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA;
DE            EC=2.7.6.5;
GN   OrderedLocusNames=Tcur_2116;
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   NCIMB 10081).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081;
RX   DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Djao O., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Brettin T., Han C., Detter J., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Thermomonospora curvata type strain
RT   (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY97682.1; -; Genomic_DNA.
DR   RefSeq; YP_003299720.1; NC_013510.1.
DR   ProteinModelPortal; D1AEV7; -.
DR   EnsemblBacteria; ACY97682; ACY97682; Tcur_2116.
DR   GeneID; 8603450; -.
DR   KEGG; tcu:Tcur_2116; -.
DR   PATRIC; 32513884; VBITheCur33965_2164.
DR   HOGENOM; HOG000018301; -.
DR   KO; K00951; -.
DR   OMA; LSWFREI; -.
DR   BioCyc; TCUR471852:GHHD-2160-MONOMER; -.
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   807 AA;  89821 MW;  AAFB6B9C20C0130B CRC64;
     MPGEVVSTDA VAKAPHGGGP AEPTAKSDPA RPQEAPDRSG RPPAAPSSAA APQQVAPSAA
     PPSAARVRRR LARLGAQRGT TMNPVLEPLI RTVRNTHPKA DIRLIERAYE VAAYYHRDQK
     RKSGDPYITH PLAVTTILAE LGMNTETLCA ALLHDTIEDT EYTLEELREE FGEEIASLVD
     GVTKLDKVKY GDAAEAETVR KMVVAMARDI RVLVIKLADR LHNMRTLRYM PRHKQEKKAR
     ETLEVFAPLA HRLGMNTLKW ELEDLAFATL YPKRFDEIAR LVSERAPRRD VYLTEVIDKV
     SADLREAKIK ATVTGRPKHY YSIYQKMIAR NVGFDEIYDL VGIRVLVDTV RDCYATLGTI
     HARWNPVPGR FKDYIAMPKF NMYQSLHTTV IGPEGKPVEL QIRTWGMHRR AEYGVAAHWK
     YKEETVGGRK AADMQWLKQL LDWQKETADP AEFLEGLRFD LSVSEVFVFT PKGDVIALPQ
     GATPVDFAYA IHTEVGHRCI GARVNGRLVP LESTLDNGDL VEVFTSKSPD AGPSRDWLNF
     VKSARARNKI KHWFTKERRD TAIEAGKESI ARAMRKQNMP LQRMMSGEAL LALARDMRYP
     DVSALYAAVG EGHVSAQAVV QRLVEALGGV ESAEEDMAEV AVPTRRRRRS RPAGDPGVVV
     AGGDPDVWVR LSRCCTPVPG DEIVGFVTRG HGVSVHRTDC GNVANLRNQP DRLIDVKWSP
     SEDSVFLVSI QMEALDRPRL LSDVTRVLSD QHVNILSASV TTTRDRVAVS RFTFEMGDPK
     HLGHVLKAVR SVDGVYDVYR VTSGGGR
//