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Database: UniProt
Entry: P0C0U4
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Original site: P0C0U4 
ID   RIMK_ECOLI              Reviewed;         300 AA.
AC   P0C0U4; P17116; P75814;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   13-FEB-2019, entry version 104.
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=Polyglutamate synthase;
DE   AltName: Full=Ribosomal protein S6 modification protein {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK; OrderedLocusNames=b0852, JW0836;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
RC   STRAIN=K12;
RX   PubMed=2570347; DOI=10.1007/BF02464894;
RA   Kang W.-K., Icho T., Isono S., Kitakawa M., Isono K.;
RT   "Characterization of the gene rimK responsible for the addition of
RT   glutamic acid residues to the C-terminus of ribosomal protein S6 in
RT   Escherichia coli K12.";
RL   Mol. Gen. Genet. 217:281-288(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   AND BIOTECHNOLOGY.
RC   STRAIN=K12;
RX   PubMed=21278279; DOI=10.1128/AEM.02043-10;
RA   Kino K., Arai T., Arimura Y.;
RT   "Poly-alpha-glutamic acid synthesis using a novel catalytic activity
RT   of RimK from Escherichia coli K-12.";
RL   Appl. Environ. Microbiol. 77:2019-2025(2011).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH ADP, AND
RP   SUBUNIT.
RX   PubMed=23609986; DOI=10.1002/prot.24311;
RA   Zhao G., Jin Z., Wang Y., Allewell N.M., Tuchman M., Shi D.;
RT   "Structure and function of Escherichia coli RimK, an ATP-grasp fold,
RT   L-glutamyl ligase enzyme.";
RL   Proteins 81:1847-1854(2013).
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       ECO:0000269|PubMed:21278279, ECO:0000269|PubMed:2570347}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5 for RpsF modification and 9 for polyglutamate
CC         synthase activity. {ECO:0000269|PubMed:21278279};
CC       Temperature dependence:
CC         Shows thermal stability. Exhibits 86% activity after incubation
CC         at 55 degrees Celsius for 15 minutes, but its activity decreases
CC         sharply at 60 degrees Celsius. {ECO:0000269|PubMed:21278279};
CC   -!- BIOTECHNOLOGY: This protein may find application in fermentative
CC       methods that use microorganisms overexpressing rimK for mass
CC       production of poly-alpha-amino acids, which is thought to be the
CC       most economical and ecofriendly manufacturing process.
CC       {ECO:0000269|PubMed:21278279}.
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP-
CC       Rule:MF_01552}.
DR   EMBL; X15859; CAA33868.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73939.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35563.2; -; Genomic_DNA.
DR   PIR; D64823; D64823.
DR   RefSeq; NP_415373.1; NC_000913.3.
DR   RefSeq; WP_000684321.1; NZ_LN832404.1.
DR   PDB; 4IWX; X-ray; 2.85 A; A=1-300.
DR   PDB; 4IWY; X-ray; 2.90 A; A=2-300.
DR   PDB; 5ZCT; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-292.
DR   PDBsum; 4IWX; -.
DR   PDBsum; 4IWY; -.
DR   PDBsum; 5ZCT; -.
DR   ProteinModelPortal; P0C0U4; -.
DR   SMR; P0C0U4; -.
DR   BioGrid; 4259992; 31.
DR   IntAct; P0C0U4; 4.
DR   STRING; 316385.ECDH10B_0922; -.
DR   jPOST; P0C0U4; -.
DR   PaxDb; P0C0U4; -.
DR   PRIDE; P0C0U4; -.
DR   EnsemblBacteria; AAC73939; AAC73939; b0852.
DR   EnsemblBacteria; BAA35563; BAA35563; BAA35563.
DR   GeneID; 945484; -.
DR   KEGG; ecj:JW0836; -.
DR   KEGG; eco:b0852; -.
DR   PATRIC; fig|1411691.4.peg.1426; -.
DR   EchoBASE; EB0845; -.
DR   EcoGene; EG10852; rimK.
DR   eggNOG; ENOG4105D9I; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000293092; -.
DR   InParanoid; P0C0U4; -.
DR   KO; K05844; -.
DR   PhylomeDB; P0C0U4; -.
DR   BioCyc; EcoCyc:EG10852-MONOMER; -.
DR   BioCyc; ECOL316407:JW0836-MONOMER; -.
DR   BioCyc; MetaCyc:EG10852-MONOMER; -.
DR   PRO; PR:P0C0U4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018169; F:ribosomal S6-glutamic acid ligase activity; IDA:EcoCyc.
DR   GO; GO:0018410; P:C-terminal protein amino acid modification; IMP:EcoCyc.
DR   GO; GO:0009432; P:SOS response; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    300       Ribosomal protein S6--L-glutamate ligase.
FT                                /FTId=PRO_0000205455.
FT   DOMAIN      104    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01552}.
FT   NP_BIND     178    179       ATP. {ECO:0000305|PubMed:23609986}.
FT   NP_BIND     211    213       ATP. {ECO:0000305|PubMed:23609986}.
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:0000305|PubMed:23609986}.
FT   BINDING     187    187       ATP. {ECO:0000305|PubMed:23609986}.
FT   CONFLICT      1     18       MKIAILSRDGTLYSCKRL -> MERSIRVSGW (in Ref.
FT                                1; CAA33868). {ECO:0000305}.
FT   STRAND        2      8       {ECO:0000244|PDB:5ZCT}.
FT   HELIX        13     24       {ECO:0000244|PDB:5ZCT}.
FT   STRAND       28     32       {ECO:0000244|PDB:5ZCT}.
FT   HELIX        34     36       {ECO:0000244|PDB:5ZCT}.
FT   STRAND       37     43       {ECO:0000244|PDB:5ZCT}.
FT   STRAND       48     50       {ECO:0000244|PDB:5ZCT}.
FT   STRAND       59     64       {ECO:0000244|PDB:5ZCT}.
FT   HELIX        67     69       {ECO:0000244|PDB:5ZCT}.
FT   HELIX        70     82       {ECO:0000244|PDB:5ZCT}.
FT   STRAND       86     89       {ECO:0000244|PDB:5ZCT}.
FT   HELIX        91     98       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       100    109       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      117    122       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       126    133       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      135    142       {ECO:0000244|PDB:5ZCT}.
FT   TURN        147    150       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      151    154       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       157    168       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       170    172       {ECO:0000244|PDB:4IWX}.
FT   STRAND      174    178       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       181    183       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      186    193       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      196    204       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      207    209       {ECO:0000244|PDB:4IWX}.
FT   HELIX       214    216       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      219    222       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       227    239       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      243    252       {ECO:0000244|PDB:5ZCT}.
FT   STRAND      255    264       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       268    274       {ECO:0000244|PDB:5ZCT}.
FT   HELIX       278    289       {ECO:0000244|PDB:5ZCT}.
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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