GenomeNet

Database: UniProt
Entry: B1X7Z3
LinkDB: B1X7Z3
Original site: B1X7Z3 
ID   RIMK_ECODH              Reviewed;         300 AA.
AC   B1X7Z3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-DEC-2018, entry version 67.
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=ECDH10B_0922;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(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; CP000948; ACB02053.1; -; Genomic_DNA.
DR   RefSeq; WP_000684321.1; NC_010473.1.
DR   ProteinModelPortal; B1X7Z3; -.
DR   SMR; B1X7Z3; -.
DR   EnsemblBacteria; ACB02053; ACB02053; ECDH10B_0922.
DR   KEGG; ecd:ECDH10B_0922; -.
DR   eggNOG; ENOG4105D9I; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
DR   BioCyc; ECOL316385:ECDH10B_RS04725-MONOMER; -.
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; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    300       Ribosomal protein S6--L-glutamate ligase.
FT                                /FTId=PRO_1000146933.
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;  32436 MW;  C0AF021292ED41DD CRC64;
     MKIAILSRDG TLYSCKRLRE AAIQRGHLVE ILDPLSCYMN INPAASSIHY KGRKLPHFDA
     VIPRIGTAIT FYGTAALRQF EMLGSYPLNE SVAIARARDK LRSMQLLARQ GIDLPVTGIA
     HSPDDTSDLI DMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAHILVQEYI
     KEAQGCDIRC LVVGDEVVAA IERRAKEGDF RSNLHRGGAA SVASITPQER EIAIKAARTM
     ALDVAGVDIL RANRGPLVME VNASPGLEGI EKTTGIDIAG KMIRWIERHA TTEYCLKTGG
//
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