Entry bact:RELA_ECOLI

ID   RELA_ECOLI              Reviewed;         744 AA.
AC   P0AG20; P11585; Q2MA48;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   15-FEB-2017, entry version 96.
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=b2784, JW2755;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2844820;
RA   Metzger S., Dror I.B., Aizenman E., Schreiber G., Toone M.,
RA   Friesen J.D., Cashel M., Glaser G.;
RT   "The nucleotide sequence and characterization of the relA gene of
RT   Escherichia coli.";
RL   J. Biol. Chem. 263:15699-15704(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION IN PERSISTENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=14622409; DOI=10.1046/j.1365-2958.2003.03779.x;
RA   Korch S.B., Henderson T.A., Hill T.M.;
RT   "Characterization of the hipA7 allele of Escherichia coli and evidence
RT   that high persistence is governed by (p)ppGpp synthesis.";
RL   Mol. Microbiol. 50:1199-1213(2003).
RN   [5]
RP   FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / AB400;
RX   PubMed=19460094; DOI=10.1111/j.1365-2958.2009.06739.x;
RA   Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F.,
RA   Ritz D., Keck W., Ackermann M., Schirmer T., Jenal U.;
RT   "Second messenger signalling governs Escherichia coli biofilm
RT   induction upon ribosomal stress.";
RL   Mol. Microbiol. 72:1500-1516(2009).
RN   [6]
RP   FUNCTION IN PERSISTENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=26051177; DOI=10.1016/j.molcel.2015.05.011;
RA   Verstraeten N., Knapen W.J., Kint C.I., Liebens V., Van den Bergh B.,
RA   Dewachter L., Michiels J.E., Fu Q., David C.C., Fierro A.C.,
RA   Marchal K., Beirlant J., Versees W., Hofkens J., Jansen M.,
RA   Fauvart M., Michiels J.;
RT   "Obg and membrane depolarization are part of a microbial bet-hedging
RT   strategy that leads to antibiotic tolerance.";
RL   Mol. Cell 59:9-21(2015).
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.
CC       {ECO:0000269|PubMed:14622409, ECO:0000269|PubMed:19460094,
CC       ECO:0000269|PubMed:26051177}.
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   -!- DISRUPTION PHENOTYPE: A slight increase in biofilm formation in a
CC       csrA-disrupted background; when combined with a spoT disruption (a
CC       ppGpp0 mutant) there is a very large increase in biofilm formation
CC       (PubMed:19460094). Deletion of relA alone decreases persister cell
CC       formation in a hipA7 mutant; the double relA/spoT deletion
CC       obviates persister cell formation (PubMed:14622409,
CC       PubMed:26051177). {ECO:0000269|PubMed:14622409,
CC       ECO:0000269|PubMed:19460094, ECO:0000269|PubMed:26051177}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; J04039; AAA03237.1; -; Unassigned_DNA.
DR   EMBL; U29580; AAA69294.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75826.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76858.1; -; Genomic_DNA.
DR   PIR; D65060; KIECG.
DR   RefSeq; NP_417264.1; NC_000913.3.
DR   RefSeq; WP_000226815.1; NZ_LN832404.1.
DR   PDB; 5IQR; EM; 3.00 A; 8=1-744.
DR   PDB; 5KPS; EM; 3.90 A; A=2-744.
DR   PDB; 5KPV; EM; 4.10 A; 33=2-744.
DR   PDB; 5KPW; EM; 3.90 A; 33=2-744.
DR   PDB; 5KPX; EM; 3.90 A; 33=2-744.
DR   PDB; 5L3P; EM; 3.70 A; z=1-744.
DR   PDBsum; 5IQR; -.
DR   PDBsum; 5KPS; -.
DR   PDBsum; 5KPV; -.
DR   PDBsum; 5KPW; -.
DR   PDBsum; 5KPX; -.
DR   PDBsum; 5L3P; -.
DR   ProteinModelPortal; P0AG20; -.
DR   SMR; P0AG20; -.
DR   BioGrid; 4259226; 67.
DR   DIP; DIP-10658N; -.
DR   IntAct; P0AG20; 15.
DR   STRING; 511145.b2784; -.
DR   ChEMBL; CHEMBL1163114; -.
DR   EPD; P0AG20; -.
DR   PaxDb; P0AG20; -.
DR   PRIDE; P0AG20; -.
DR   EnsemblBacteria; AAC75826; AAC75826; b2784.
DR   EnsemblBacteria; BAE76858; BAE76858; BAE76858.
DR   GeneID; 947244; -.
DR   KEGG; ecj:JW2755; -.
DR   KEGG; eco:b2784; -.
DR   PATRIC; 32120984; VBIEscCol129921_2884.
DR   EchoBASE; EB0828; -.
DR   EcoGene; EG10835; relA.
DR   eggNOG; ENOG4105CWR; Bacteria.
DR   eggNOG; COG0317; LUCA.
DR   HOGENOM; HOG000018300; -.
DR   InParanoid; P0AG20; -.
DR   KO; K00951; -.
DR   OMA; TEIGHNC; -.
DR   PhylomeDB; P0AG20; -.
DR   BioCyc; EcoCyc:RELA-MONOMER; -.
DR   BioCyc; MetaCyc:RELA-MONOMER; -.
DR   UniPathway; UPA00908; UER00884.
DR   PRO; PR:P0AG20; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:EcoCyc.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IMP:EcoCyc.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoCyc.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; GTP-binding; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    744       GTP pyrophosphokinase.
FT                                /FTId=PRO_0000166546.
FT   DOMAIN      668    743       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   CONFLICT    307    307       F -> K (in Ref. 1; AAA03237).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       406    465       ipfam:TGS [T]
FT   MYHIT       251    360       ipfam:RelA_SpoT [T]
FT   MYHIT       668    743       iprf:ACT [T]
FT   MYHIT        44    191       ipfam:HD_4 [T]
FT   MYHIT       251    361       ismart:RelA_SpoT [T]
FT   MYHIT       664    740       ipfam:ACT_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
//