GenomeNet

Database: UniProt
Entry: A7ZJS0
LinkDB: A7ZJS0
Original site: A7ZJS0 
ID   RIMK_ECO24              Reviewed;         300 AA.
AC   A7ZJS0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   10-OCT-2018, entry version 69.
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=EcE24377A_0924;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV19505.1; -; Genomic_DNA.
DR   RefSeq; WP_000684336.1; NC_009801.1.
DR   ProteinModelPortal; A7ZJS0; -.
DR   SMR; A7ZJS0; -.
DR   PRIDE; A7ZJS0; -.
DR   EnsemblBacteria; ABV19505; ABV19505; EcE24377A_0924.
DR   KEGG; ecw:EcE24377A_0924; -.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
DR   Proteomes; UP000001122; 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.
FT   CHAIN         1    300       Ribosomal protein S6--L-glutamate ligase.
FT                                /FTId=PRO_1000068834.
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}.
SQ   SEQUENCE   300 AA;  32463 MW;  35B5B21292F7F1D6 CRC64;
     MKIAILSRDG TLYSCKRLRE AAIQRGHLVE ILDPLSCYMN INPAASSIHY KGRKLPHFDA
     VIPRIGTAIT FYGTAALRQF EMLGSYPLNE SVAIARARDK LRSMQLLARQ GIDLPVTGIA
     HSPDDTSDLI DMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAYILVQEYI
     KEAQGCDIRC LVVGDEVVAA IERRAKEGDF RSNLHRGGAA SVASITPQER EIAIKAARTM
     ALDVAGVDIL RANRGPLVME VNASPGLEGI EKTTGIDIAG KMIRWIERHA TTEYCLKTGG
//
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