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Database: UniProt/TrEMBL
Entry: B8DHM5_LISMH
LinkDB: B8DHM5_LISMH
Original site: B8DHM5_LISMH 
ID   B8DHM5_LISMH            Unreviewed;       738 AA.
AC   B8DHM5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   14-MAY-2014, entry version 39.
DE   SubName: Full=GTP pyrophosphokinase (ATP:GTP 3-pyrophosphotransferase)(PpGpp synthetase I) ((P)ppGpp synthetase);
DE            EC=2.7.6.5;
GN   OrderedLocusNames=LMHCC_1046;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/JB.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T.,
RA   Bridges S.M., Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(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.
CC   -!- SIMILARITY: Contains HD domain.
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DR   EMBL; CP001175; ACK39394.1; -; Genomic_DNA.
DR   RefSeq; YP_002350008.1; NC_011660.1.
DR   STRING; 552536.LMHCC_1046; -.
DR   EnsemblBacteria; ACK39394; ACK39394; LMHCC_1046.
DR   GeneID; 7079979; -.
DR   KEGG; lmh:LMHCC_1046; -.
DR   PATRIC; 20317209; VBILisMon86872_1035.
DR   eggNOG; COG0317; -.
DR   HOGENOM; HOG000018300; -.
DR   KO; K00951; -.
DR   OMA; IGYITRG; -.
DR   OrthoDB; EOG6SV551; -.
DR   BioCyc; LMON552536:GIW4-1082-MONOMER; -.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-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; IPR002912; ACT_dom.
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   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Kinase; Transferase.
SQ   SEQUENCE   738 AA;  84760 MW;  AE9ED99C50205203 CRC64;
     MAKEQNLTAE QVIDMASHYM NQEHLALVKK AYEFARDSHK EQFRKSGEPY IIHPIQVAGI
     LVELKMDPST VASGFLHDVV EDTPVTLADL EEVFGSEVAM 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 IRQLGFESKK IMTPENLRKL ADKLNFSHED DLFAAVGYNG
     ITALQVANRL TEKLRKEREL EAETEKLLTQ SENKPSNSDA NNEKLKIKHN AGVVVQGVGN
     LLIRLSRCCN PVPGDDIVGY ITKGRGISIH RQDCPNVQAI EPERLIEVDW EDADSQAKND
     YNVDIEIYGY NRNGLLNDIL QVINSLTSNI NGVNAKVDNN KMATLVVTLQ IHNINHLQRV
     VDKIKQIPDV YTVRRLMN
//
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