RELA_SHIFL
ID RELA_SHIFL Reviewed; 744 AA.
AC P0AG23; P11585;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SF2797, S2991;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC This enzyme catalyzes the formation of pppGpp which is then hydrolyzed
CC to form ppGpp (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44285.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18110.1; -; Genomic_DNA.
DR RefSeq; NP_708578.1; NC_004337.2.
DR RefSeq; WP_000226815.1; NZ_WPGW01000063.1.
DR AlphaFoldDB; P0AG23; -.
DR SMR; P0AG23; -.
DR STRING; 198214.SF2797; -.
DR PRIDE; P0AG23; -.
DR EnsemblBacteria; AAN44285; AAN44285; SF2797.
DR EnsemblBacteria; AAP18110; AAP18110; S2991.
DR GeneID; 1027604; -.
DR GeneID; 66673349; -.
DR KEGG; sfl:SF2797; -.
DR KEGG; sfx:S2991; -.
DR PATRIC; fig|198214.7.peg.3330; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OMA; TEIGHNC; -.
DR OrthoDB; 204079at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF19296; DUF5913; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00691; spoT_relA; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..744
FT /note="GTP pyrophosphokinase"
FT /id="PRO_0000166554"
FT DOMAIN 55..160
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 404..465
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 668..743
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
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
