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Database: UniProt
Entry: Q83S18
LinkDB: Q83S18
Original site: Q83S18 
ID   RIMK_SHIFL              Reviewed;         300 AA.
AC   Q83S18; Q7UD77;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   07-NOV-2018, entry version 102.
DE   RecName: Full=Ribosomal protein S6--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
DE   AltName: Full=Poly-alpha-glutamate synthase {ECO:0000255|HAMAP-Rule:MF_01552};
DE   AltName: Full=Ribosomal protein S6 modification protein {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552};
GN   OrderedLocusNames=SF0806, S0848;
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.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   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.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Is an L-glutamate ligase that catalyzes the ATP-
CC       dependent post-translational addition of glutamate residues to the
CC       C-terminus of ribosomal protein S6 (RpsF). Is also able to
CC       catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP
CC       hydrolysis from unprotected glutamate as substrate. The number of
CC       glutamate residues added to either RpsF or to poly-alpha-glutamate
CC       changes with pH. {ECO:0000255|HAMAP-Rule:MF_01552}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01552};
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP-
CC       Rule:MF_01552}.
DR   EMBL; AE005674; AAN42439.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16311.1; -; Genomic_DNA.
DR   RefSeq; NP_706732.1; NC_004337.2.
DR   ProteinModelPortal; Q83S18; -.
DR   SMR; Q83S18; -.
DR   EnsemblBacteria; AAN42439; AAN42439; SF0806.
DR   EnsemblBacteria; AAP16311; AAP16311; S0848.
DR   GeneID; 1026162; -.
DR   KEGG; sfl:SF0806; -.
DR   KEGG; sfx:S0848; -.
DR   PATRIC; fig|198214.7.peg.934; -.
DR   eggNOG; ENOG4105D9I; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018169; F:ribosomal S6-glutamic acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018410; P:C-terminal protein amino acid modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01552; RimK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR023533; RimK.
DR   InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   TIGRFAMs; TIGR00768; rimK_fam; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    300       Ribosomal protein S6--L-glutamate ligase.
FT                                /FTId=PRO_0000205484.
FT   DOMAIN      104    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01552}.
FT   NP_BIND     178    179       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   NP_BIND     211    213       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       248    248       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       262    262       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     141    141       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     187    187       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   CONFLICT    227    227       L -> P (in Ref. 2; AAP16311).
FT                                {ECO:0000305}.
SQ   SEQUENCE   300 AA;  32527 MW;  254A85665186FC1B CRC64;
     MKIAILSRDG TLYSCKRLRE AAIQRGHLVE ILDPLSCYMN INPAASSIYY KGRKLPHFDA
     VIPRIGTAIT FYGTAALRQF EMLGSYPLNE SVAIARARDK LRSMQLLARQ GIDLPVTGIA
     HSPDDTSDLI DMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAHILVQEYI
     KEAQGCDIRC LVVGDEVVAA IERRAKEGYF RSNLHRGGAA SVASITLQER EIAIKAARTM
     ALDVAGVDIL RANRGPLVME VNASPGLEGI EKTTGIDIAG KMIRWIERHA TTEYCLKTGG
//
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