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Database: UniProt
Entry: P0A2U2
LinkDB: P0A2U2
Original site: P0A2U2 
ID   RIMK_SALTY              Reviewed;         300 AA.
AC   P0A2U2; Q9Z5Z1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=STM0875;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC   STRAIN=ATCC 29629 / TA 1535;
RA   Lambert I.B., Boroumandi S., Nokhbeh M.R., Pokorny N.S., Koziarz P.;
RT   "Cloning and characterization of the major nitrotreductase from
RT   Salmonella typhimurium TA1535.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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; AE006468; AAL19811.1; -; Genomic_DNA.
DR   EMBL; AF117952; AAD18028.1; -; Genomic_DNA.
DR   RefSeq; NP_459852.1; NC_003197.2.
DR   RefSeq; WP_000684361.1; NC_003197.2.
DR   ProteinModelPortal; P0A2U2; -.
DR   SMR; P0A2U2; -.
DR   STRING; 99287.STM0875; -.
DR   PaxDb; P0A2U2; -.
DR   EnsemblBacteria; AAL19811; AAL19811; STM0875.
DR   GeneID; 1252394; -.
DR   KEGG; stm:STM0875; -.
DR   PATRIC; fig|99287.12.peg.914; -.
DR   eggNOG; ENOG4105D9I; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
DR   PhylomeDB; P0A2U2; -.
DR   BioCyc; SENT99287:STM0875-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018410; P:C-terminal protein amino acid modification; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IBA:GO_Central.
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_0000205481.
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     26     26       G -> R (in Ref. 2; AAD18028).
FT                                {ECO:0000305}.
SQ   SEQUENCE   300 AA;  32294 MW;  E926DF12A50B868C CRC64;
     MKIAILSRDG TLYSCKRLRE AAMRRGHLVE ILDPLSCYMN INPAASSIHY KGRRLPHFDA
     VIPRIGSAIT FYGTAALRQF ELLGSYPLNE SVAITRARDK LRSLQLLARQ GIDLPITGIA
     HSPDDTSDLI KMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAHILVQEYI
     AEAKGCDIRC LVVGNEVVAA IERCAKAGDF RSNLHRGGVA SIATITPRER DIAIKAAQTL
     GLDVAGVDIL RAARGPLVME VNASPGLEGI EKTTGVDIAG RMIQWIERHA TPEFCLKIGG
//
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