ID   D3UNA6_LISSS            Unreviewed;       738 AA.
AC   D3UNA6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   01-MAY-2013, entry version 28.
DE   SubName: Full=GTP pyrophosphokinase;
DE            EC=2.7.6.5;
GN   Name=relA; OrderedLocusNames=lse_1438;
OS   Listeria seeligeri serovar 1/2b (strain ATCC 35967 / DSM 20751 / CIP
OS   100100 / SLCC 3954).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=683837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35967 / DSM 20751 / CIP 100100 / SLCC 3954;
RX   PubMed=20061480; DOI=10.1128/JB.01415-09;
RA   Steinweg C., Kuenne C.T., Billion A., Mraheil M.A., Domann E.,
RA   Ghai R., Barbuddhe S.B., Karst U., Goesmann A., Puhler A.,
RA   Weisshaar B., Wehland J., Lampidis R., Kreft J., Goebel W.,
RA   Chakraborty T., Hain T.;
RT   "Complete genome sequence of Listeria seeligeri, a nonpathogenic
RT   member of the genus Listeria.";
RL   J. Bacteriol. 192:1473-1474(2010).
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; FN557490; CBH27589.1; -; Genomic_DNA.
DR   RefSeq; YP_003464675.1; NC_013891.1.
DR   ProteinModelPortal; D3UNA6; -.
DR   EnsemblBacteria; CBH27589; CBH27589; lse_1438.
DR   GeneID; 9082392; -.
DR   KEGG; lsg:lse_1438; -.
DR   PATRIC; 32262775; VBILisSee138575_1434.
DR   HOGENOM; HOG000018300; -.
DR   KO; K00951; -.
DR   BioCyc; LSEE683837:GI10-2596-MONOMER; -.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; Kinase; Transferase.
SQ   SEQUENCE   738 AA;  84784 MW;  DE9940486FD2BA9A CRC64;
     MAKEQNLTAE QVIDMASHYM NQEHLALVKK AYEFARDSHK EQFRKSGEPY IIHPIQVAGI
     LVELKMDPST VASGFLHDVV EDTPVTLADL EEEFGSEVAM LVDGVTKLGK IKYKSHEEQQ
     AENHRKMFIA MAQDIRVILI KLADRLHNMR TLKHLPVEKQ RRIANETLEI FAPLAHRLGI
     SRVKWELEDT ALRYLNPQQY YRIVHLMKQK RDARERYLHD VIDGVNENLD ELNIQADISG
     RPKHIYSIYR KMSEQNKQFN EIYDLLAVRI VVSSIKDCYA VLGIIHTRWK PMPGRFKDYI
     AMPKSNMYQS IHTTVIGPQG EPLEVQIRTH EMHQIAEYGV AAHWAYKEGK VVNSKTSFDN
     KLTWFREILE YQNESDNAEE FMESLKLDLF SDVVYVFTPK GDVYELPNGS VPLDFAYRVH
     TEIGNKTIGA KINGKIVTLD YKLKTGDIID ILTSKHSYGP SRDWLKLVQT SQARNKIKQF
     FKRQAKEENV EKGRDLVEKE IRQLGFEPKK IMLPENLRKL ADKLNFSHED DLFAAVGYNG
     ITALQVANRL TEKLRKEREL EAETEKLLTQ AENKPSNSDA NNEKLKIKHN AGVVVQGVGN
     LLIRLSRCCN PVPGDEIVGY ITKGRGISIH RQDCPNVQAI EAERLIEVDW EDADSQAKND
     YNVDIEIYGY NRNGLLNDIL QVINSLTSNI NGVNAKVDNN KMATLVVTLQ IHNINHLQRV
     VDKIKQIPDV YTVRRLMN
//