ID   A4TBS1_MYCGI            Unreviewed;       790 AA.
AC   A4TBS1;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   01-MAY-2013, entry version 45.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA;
DE            EC=2.7.6.5;
GN   OrderedLocusNames=Mflv_3812;
OS   Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens
OS   (strain ATCC 700033 / PYR-GCK)).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000656; ABP46284.1; -; Genomic_DNA.
DR   RefSeq; YP_001135072.1; NC_009338.1.
DR   ProteinModelPortal; A4TBS1; -.
DR   STRING; 350054.Mflv_3812; -.
DR   EnsemblBacteria; ABP46284; ABP46284; Mflv_3812.
DR   GeneID; 4975128; -.
DR   KEGG; mgi:Mflv_3812; -.
DR   PATRIC; 18035799; VBIMycGil17082_3874.
DR   eggNOG; COG0317; -.
DR   HOGENOM; HOG000018301; -.
DR   KO; K00951; -.
DR   OMA; VEDTGYS; -.
DR   ProtClustDB; CLSK791939; -.
DR   BioCyc; MGIL350054:GHK8-4209-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   790 AA;  87160 MW;  4571444222392033 CRC64;
     MADKVRTDPG SGQAVQTPPP AASASPETQP MEIVKPAPTS ASRRVRARLA RRMTSQRSTV
     NPVLEPLVAV HREIYPKADL TLLQKAYEVA EQRHADQLRK SGDPYITHPL AVANILAELG
     MDTTTLIAAL LHDTVEDTGY TLEALTQEFG VEVGHLVDGV TKLDKVALGT AAEGETIRKM
     IIAMARDPRV LVIKVADRLH NMRTMRFLPP EKQARKARET LEVIAPLAHR LGMATVKWEL
     EDLSFAILHP KKYEEIVRLV ADRAPSRDTY LAKVRAEITA TLNASKIKAT VEGRPKHYWS
     IYQKMIVKGR DFDDIHDLVG VRILCDEVRD CYAAVGVVHS LWQPIAGRFK DYIAQPRFGV
     YQSLHTTVVG PEGKPLEVQI RTIDMHKTAE YGIAAHWRYK EVKGRNGVPA GSAATEIDDM
     AWMRQLLDWQ REAADPGEFL ESLRYDLAVQ EIFVFTPKGD VITLPTGSTP VDFAYAVHTE
     VGHRCIGARV NGRLVALERK LENGEVVEVF TSKAQNAGPS RDWQGFVVSP RAKAKIRQWF
     AKERREEALD SGKEAIAREV RRGGLPLQRL MNAETMAALA RELRYLDVSA LYTAVGEGHV
     SARHVVQRLV AQLGGDDEAA DELAERSTPA TMPIRQRTSD DVGVAVPGAP GVLTKLAKCC
     TPVPGDNILG FVTRGGGVSV HRTDCTNAAS LEQQSERIID VQWAPSPSSV FLVAIQVEAL
     DRHRLLSDVT RVLADEKVNI LSASVTTSND RVAISRFTFE MGDPKHLGHV LNVVRNVEGV
     YDVYRVTSAA
//