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Database: UniProt/TrEMBL
Entry: A5ITF8_STAA9
LinkDB: A5ITF8_STAA9
Original site: A5ITF8_STAA9 
ID   A5ITF8_STAA9            Unreviewed;       729 AA.
AC   A5ITF8;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   19-FEB-2014, entry version 47.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA;
DE            EC=2.7.6.5;
GN   OrderedLocusNames=SaurJH9_1691;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH9;
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., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp.
RT   aureus JH9.";
RL   Submitted (MAY-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.
CC   -!- SIMILARITY: Contains HD domain.
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DR   EMBL; CP000703; ABQ49481.1; -; Genomic_DNA.
DR   RefSeq; YP_001247057.1; NC_009487.1.
DR   ProteinModelPortal; A5ITF8; -.
DR   SMR; A5ITF8; 7-350.
DR   STRING; 359786.SaurJH9_1691; -.
DR   EnsemblBacteria; ABQ49481; ABQ49481; SaurJH9_1691.
DR   GeneID; 5168887; -.
DR   KEGG; saj:SaurJH9_1691; -.
DR   PATRIC; 19541200; VBIStaAur42398_1791.
DR   eggNOG; COG0317; -.
DR   HOGENOM; HOG000018301; -.
DR   KO; K00951; -.
DR   OMA; LDWLNFV; -.
DR   OrthoDB; EOG6SV551; -.
DR   ProtClustDB; CLSK885475; -.
DR   BioCyc; SAUR359786:GJEM-1718-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:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR026020; (p)ppGpp_Synthase.
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   PANTHER; PTHR21262:SF1; PTHR21262:SF1; 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; SSF81271; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Transferase.
SQ   SEQUENCE   729 AA;  83722 MW;  F1CC2F741952100E CRC64;
     MNNEYPYSAD EVLHKAKSYL SADEYEYVLK SYHIAYEAHK GQFRKNGLPY IMHPIQVAGI
     LTEMRLDGPT IVAGFLHDVI EDTPYTFEDV KEMFNEEVAR IVDGVTKLKK VKYRSKEEQQ
     AENHRKLFIA IAKDVRVILV KLADRLHNMR TLKAMPREKQ IRISRETLEI YAPLAHRLGI
     NTIKWELEDT ALRYIDNVQY FRIVNLMKKK RSEREAYIET AIDRIRTEMD RMNIEGDING
     RPKHIYSIYR KMMKQKKQFD QIFDLLAIRV IVNSINDCYA ILGLVHTLWK PMPGRFKDYI
     AMPKQNLYQS LHTTVVGPNG DPLEIQIRTF DMHEIAEHGV AAHWAYKEGK KVSEKDQTYQ
     NKLNWLKELA EADHTSSDAQ EFMETLKYDL QSDKVYAFTP ASDVIELPYG AVPIDFAYAI
     HSEVGNKMIG AKVNGKIVPI DYILQTGDIV EIRTSKHSYG PSRDWLKIVK SSSAKGKIKS
     FFKKQDRSSN IEKGRMMVEV EIKEQGFRVE DILTEKNIQV VNEKYNFANE DDLFAAVGFG
     GVTSLQIVNK LTERQRILDK QRALNEAQEV TKSLPIKDNI ITDSGVYVEG LENVLIKLSK
     CCNPIPGDDI VGYITKGHGI KVHRTDCPNI KNETERLINV EWVKSKDATQ KYQVDLEVTA
     YDRNGLLNEV LQAVSSTAGN LIKVSGRSDI DKNAIINISV MVKNVNDVYR VVEKIKQLGD
     VYTVTRVWN
//
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