Entry sw:RELA_ECO57

ID   RELA_ECO57              Reviewed;         744 AA.
AC   P0AG22; P11585;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   02-NOV-2016, entry version 79.
DE   RecName: Full=GTP pyrophosphokinase;
DE            EC=2.7.6.5;
DE   AltName: Full=(p)ppGpp synthase;
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
DE   AltName: Full=ppGpp synthase I;
GN   Name=relA; OrderedLocusNames=Z4099, ECs3644;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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. This enzyme catalyzes the
CC       formation of pppGpp which is then hydrolyzed to form ppGpp (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-
CC       triphosphate.
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP:
CC       step 1/2.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU01007}.
DR   EMBL; AE005174; AAG57897.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37067.1; -; Genomic_DNA.
DR   PIR; D91084; D91084.
DR   PIR; E85929; E85929.
DR   RefSeq; NP_311671.1; NC_002695.1.
DR   RefSeq; WP_000226815.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; P0AG22; -.
DR   SMR; P0AG22; -.
DR   STRING; 155864.Z4099; -.
DR   PRIDE; P0AG22; -.
DR   DNASU; 958253; -.
DR   EnsemblBacteria; AAG57897; AAG57897; Z4099.
DR   EnsemblBacteria; BAB37067; BAB37067; BAB37067.
DR   GeneID; 916555; -.
DR   KEGG; ece:Z4099; -.
DR   KEGG; ecs:ECs3644; -.
DR   PATRIC; 18356763; VBIEscCol44059_3564.
DR   eggNOG; ENOG4105CWR; Bacteria.
DR   eggNOG; COG0317; LUCA.
DR   HOGENOM; HOG000018300; -.
DR   KO; K00951; -.
DR   OMA; TEIGHNC; -.
DR   BioCyc; ECOO157:RELA-MONOMER; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RelA_SpoT; 1.
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   InterPro; IPR033655; TGS_RelA.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 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   ATP-binding; Complete proteome; GTP-binding; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    744       GTP pyrophosphokinase.
FT                                /FTId=PRO_0000166547.
FT   DOMAIN      668    743       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       668    743       iprf:ACT [T]
FT   MYHIT       251    360       ipfam:RelA_SpoT [T]
FT   MYHIT       251    361       ismart:RelA_SpoT [T]
FT   MYHIT       406    465       ipfam:TGS [T]
FT   MYHIT       664    740       ipfam:ACT_4 [T]
FT   MYHIT        44    191       ipfam:HD_4 [T]
SQ   SEQUENCE   744 AA;  83876 MW;  FA269709F15E1F25 CRC64;
     MVAVRSAHIN KAGEFDPEKW IASLGITSQK SCECLAETWA YCLQQTQGHP DASLLLWRGV
     EMVEILSTLS MDIDTLRAAL LFPLADANVV SEDVLRESVG KSVVNLIHGV RDMAAIRQLK
     ATHTDSVSSE QVDNVRRMLL AMVDDFRCVV IKLAERIAHL REVKDAPEDE RVLAAKECTN
     IYAPLANRLG IGQLKWELED YCFRYLHPTE YKRIAKLLHE RRLDREHYIE EFVGHLRAEM
     KAEGVKAEVY GRPKHIYSIW RKMQKKNLAF DELFDVRAVR IVAERLQDCY AALGIVHTHY
     RHLPDEFDDY VANPKPNGYQ SIHTVVLGPG GKTVEIQIRT KQMHEDAELG VAAHWKYKEG
     AAAGGARSGH EDRIAWLRKL IAWQEEMADS GEMLDEVRSQ VFDDRVYVFT PKGDVVDLPA
     GSTPLDFAYH IHSDVGHRCI GAKIGGRIVP FTYQLQMGDQ IEIITQKQPN PSRDWLNPNL
     GYVTTSRGRS KIHAWFRKQD RDKNILAGRQ ILDDELEHLG ISLKEAEKHL LPRYNFNDVD
     ELLAAIGGGD IRLNQMVNFL QSQFNKPSAE EQDAAALKQL QQKSYTPQNR SKDNGRVVVE
     GVGNLMHHIA RCCQPIPGDE IVGFITQGRG ISVHRADCEQ LAELRSHAPE RIVDAVWGES
     YSAGYSLVVR VVANDRSGLL RDITTILANE KVNVLGVASR SDTKQQLATI DMTIEIYNLQ
     VLGRVLGKLN QVPDVIDARR LHGS
//