位置:首页 > 蛋白库 > RIMM_ECOLI
RIMM_ECOLI
ID   RIMM_ECOLI              Reviewed;         182 AA.
AC   P0A7X6; P21504; Q8X9D2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Ribosome maturation factor RimM;
DE   AltName: Full=21K {ECO:0000303|PubMed:9226267};
GN   Name=rimM; Synonyms=yfjA {ECO:0000303|PubMed:9226267};
GN   OrderedLocusNames=b2608, JW5413;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RC   STRAIN=K12;
RX   PubMed=6357787; DOI=10.1002/j.1460-2075.1983.tb01519.x;
RA   Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.;
RT   "The nucleotide sequence of an Escherichia coli operon containing genes for
RT   the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a
RT   21-K polypeptide.";
RL   EMBO J. 2:899-905(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
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., Mau B.,
RA   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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   CONTROL OF TRANSLATION, AND OPERON STRUCTURE.
RX   PubMed=1569581; DOI=10.1016/0022-2836(92)90462-s;
RA   Wikstroem P.M., Lind L.K., Berg D.E., Bjoerk G.R.;
RT   "Importance of mRNA folding and start codon accessibility in the expression
RT   of genes in a ribosomal protein operon of Escherichia coli.";
RL   J. Mol. Biol. 224:949-966(1992).
RN   [6]
RP   FUNCTION, SUBUNIT, ASSOCIATION WITH 30S RIBOSOMAL SUBUNIT, SUBCELLULAR
RP   LOCATION, DISRUPTION PHENOTYPE, AND PARTIAL SUPPRESSION BY S13 MUTATIONS.
RC   STRAIN=MW100;
RX   PubMed=9226267; DOI=10.1128/jb.179.14.4567-4574.1997;
RA   Bylund G.O., Persson B.C., Lundberg L.A., Wikstroem P.M.;
RT   "A novel ribosome-associated protein is important for efficient translation
RT   in Escherichia coli.";
RL   J. Bacteriol. 179:4567-4574(1997).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PARTIAL SUPPRESSION BY RBFA
RP   OVEREXPRESSION.
RC   STRAIN=MW100;
RX   PubMed=9422595; DOI=10.1128/jb.180.1.73-82.1998;
RA   Bylund G.O., Wipemo L.C., Lundberg L.A., Wikstroem P.M.;
RT   "RimM and RbfA are essential for efficient processing of 16S rRNA in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:73-82(1998).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, FUSION WITH RIBOSOMAL PROTEIN S16, AND
RP   MUTAGENESIS OF 106-TYR-TYR-107.
RC   STRAIN=MW100;
RX   PubMed=11514519; DOI=10.1128/jb.183.18.5352-5357.2001;
RA   Loevgren J.M., Wikstroem P.M.;
RT   "Hybrid protein between ribosomal protein S16 and RimM of Escherichia coli
RT   retains the ribosome maturation function of both proteins.";
RL   J. Bacteriol. 183:5352-5357(2001).
RN   [9]
RP   INTERACTION WITH RIBOSOMAL PROTEIN S19, AND DOMAIN.
RC   STRAIN=MW100;
RX   PubMed=15496525; DOI=10.1261/rna.7720204;
RA   Loevgren J.M., Bylund G.O., Srivastava M.K., Lundberg L.A.C., Persson O.P.,
RA   Wingsle G., Wikstroem P.M.;
RT   "The PRC-barrel domain of the ribosome maturation protein RimM mediates
RT   binding to ribosomal protein S19 in the 30S ribosomal subunits.";
RL   RNA 10:1798-1812(2004).
RN   [10]
RP   FUNCTION IN 30S SUBUNIT PROTEIN ASSEMBLY.
RX   PubMed=20188109; DOI=10.1016/j.jmb.2010.02.036;
RA   Bunner A.E., Nord S., Wikstrom P.M., Williamson J.R.;
RT   "The effect of ribosome assembly cofactors on in vitro 30S subunit
RT   reconstitution.";
RL   J. Mol. Biol. 398:1-7(2010).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND STRUCTURE BY ELECTRON MICROSCOPY (15.0
RP   ANGSTROMS).
RC   STRAIN=K12 / BW25113;
RX   PubMed=23611982; DOI=10.1261/rna.037523.112;
RA   Leong V., Kent M., Jomaa A., Ortega J.;
RT   "Escherichia coli rimM and yjeQ null strains accumulate immature 30S
RT   subunits of similar structure and protein complement.";
RL   RNA 19:789-802(2013).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=27382067; DOI=10.1093/nar/gkw613;
RA   Thurlow B., Davis J.H., Leong V., Moraes T.F., Williamson J.R., Ortega J.;
RT   "Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly
RT   intermediates of the 30S subunit.";
RL   Nucleic Acids Res. 44:9918-9932(2016).
CC   -!- FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ)
CC       that assist in the late assembly stage of the 30S ribosomal subunit. An
CC       accessory protein needed during the final step in assembly of the 30S
CC       ribosomal subunit, for assembly of the head region (the 16S rRNA 3'
CC       domain) (PubMed:11514519, PubMed:15496525, PubMed:20188109,
CC       PubMed:23611982, PubMed:27382067). It may act while Era is associated
CC       and before RimP in 30S subunit assembly (PubMed:20188109). Interacts
CC       with S19 (PubMed:15496525). Essential for efficient processing of 16S
CC       rRNA; a deletion mutant accumulates 17S rRNA (PubMed:9422595).
CC       Deletions also do not assemble the head-associated ribosomal proteins
CC       correctly (PubMed:23611982, PubMed:27382067). May be needed both before
CC       and after RbfA during the maturation of 16S rRNA. It has affinity for
CC       free ribosomal 30S subunits but not for 70S ribosomes (PubMed:9226267).
CC       {ECO:0000269|PubMed:11514519, ECO:0000269|PubMed:15496525,
CC       ECO:0000269|PubMed:20188109, ECO:0000269|PubMed:23611982,
CC       ECO:0000269|PubMed:27382067, ECO:0000269|PubMed:9226267,
CC       ECO:0000269|PubMed:9422595}.
CC   -!- SUBUNIT: Binds 30S ribosomal subunit but not 70S ribosomes
CC       (PubMed:9226267). Binds ribosomal protein S19 and probably 16S rRNA
CC       (PubMed:15496525). {ECO:0000269|PubMed:15496525,
CC       ECO:0000269|PubMed:9226267}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11514519,
CC       ECO:0000269|PubMed:9226267}. Note=Binds 30S subunit, but not 70S
CC       ribosomes (PubMed:9226267). {ECO:0000269|PubMed:9226267}.
CC   -!- INDUCTION: Translation of the mRNA is repressed by a stem-loop in the
CC       first 150 nucleotides of its own transcript (PubMed:1569581). Part of
CC       the rpsP-rimM-trmD-rplS operon (PubMed:6357787, PubMed:1569581).
CC       {ECO:0000269|PubMed:1569581, ECO:0000269|PubMed:6357787}.
CC   -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19.
CC       {ECO:0000269|PubMed:15496525}.
CC   -!- DISRUPTION PHENOTYPE: Disruption causes slow growth, incomplete
CC       processing of 17S rRNA, accumulation of 30S and 50S subunits and
CC       decreased translational efficiency (PubMed:9226267, PubMed:23611982).
CC       Altered levels of ribosomal proteins in 30S subunits; S2, S3, S14 and
CC       S21 severely depleted, S5, S7 and S11 are decreased, distortion of rRNA
CC       hleix 44 near the decoding center (PubMed:23611982). Slightly different
CC       results show ribosomal proteins S2 and S21 not found in 30S subunits,
CC       decreased S3, S13 and S14 in 30S subunits (PubMed:27382067). Deletion
CC       is partially suppressed by mutations in rpsM, the gene for ribosomal
CC       protein S13 (PubMed:9226267, PubMed:15496525), by a mutation in rpsS,
CC       the gene for S19 (PubMed:15496525) and also by increased expression of
CC       RbfA (PubMed:9422595). Suppressors due to in-frame fusions with rpsP,
CC       the upstream gene for ribosomal protein S16 have been isolated
CC       (PubMed:11514519). Suppression is probably due to increased expression
CC       of RimM; the fusion proteins are found in translationally active 70S
CC       ribosomes (PubMed:11514519). {ECO:0000269|PubMed:15496525,
CC       ECO:0000269|PubMed:23611982, ECO:0000269|PubMed:27382067,
CC       ECO:0000269|PubMed:9226267, ECO:0000269|PubMed:9422595}.
CC   -!- SIMILARITY: Belongs to the RimM family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X01818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U00096; AAC75657.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16493.2; -; Genomic_DNA.
DR   PIR; C65039; C65039.
DR   RefSeq; NP_417099.4; NC_000913.3.
DR   RefSeq; WP_000043335.1; NZ_STEB01000040.1.
DR   AlphaFoldDB; P0A7X6; -.
DR   SMR; P0A7X6; -.
DR   BioGRID; 4263071; 78.
DR   BioGRID; 851436; 6.
DR   IntAct; P0A7X6; 7.
DR   STRING; 511145.b2608; -.
DR   SWISS-2DPAGE; P0A7X6; -.
DR   jPOST; P0A7X6; -.
DR   PaxDb; P0A7X6; -.
DR   PRIDE; P0A7X6; -.
DR   EnsemblBacteria; AAC75657; AAC75657; b2608.
DR   EnsemblBacteria; BAA16493; BAA16493; BAA16493.
DR   GeneID; 67414074; -.
DR   GeneID; 947101; -.
DR   KEGG; ecj:JW5413; -.
DR   KEGG; eco:b2608; -.
DR   PATRIC; fig|1411691.4.peg.4131; -.
DR   EchoBASE; EB1142; -.
DR   eggNOG; COG0806; Bacteria.
DR   HOGENOM; CLU_077636_1_0_6; -.
DR   InParanoid; P0A7X6; -.
DR   OMA; DEFYHAD; -.
DR   PhylomeDB; P0A7X6; -.
DR   BioCyc; EcoCyc:EG11153-MON; -.
DR   PRO; PR:P0A7X6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IMP:EcoliWiki.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IMP:EcoCyc.
DR   Gene3D; 2.40.30.60; -; 1.
DR   HAMAP; MF_00014; Ribosome_mat_RimM; 1.
DR   InterPro; IPR011961; 16S_RimM.
DR   InterPro; IPR027275; PRC-brl_dom.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   InterPro; IPR002676; RimM_N.
DR   InterPro; IPR036976; RimM_N_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   Pfam; PF05239; PRC; 1.
DR   Pfam; PF01782; RimM; 1.
DR   SUPFAM; SSF50346; SSF50346; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR02273; 16S_RimM; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..182
FT                   /note="Ribosome maturation factor RimM"
FT                   /id="PRO_0000163286"
FT   DOMAIN          103..182
FT                   /note="PRC barrel"
FT   MUTAGEN         106..107
FT                   /note="YY->AA: 3-fold decreased growth rate; loss of
FT                   association with 30S ribosomal subunit; loss of interaction
FT                   with S19."
FT                   /evidence="ECO:0000269|PubMed:11514519"
SQ   SEQUENCE   182 AA;  20605 MW;  D8512AB9E4FD3D75 CRC64;
     MSKQLTAQAP VDPIVLGKMG SSYGIRGWLR VFSSTEDAES IFDYQPWFIQ KAGQWQQVQL
     ESWKHHNQDM IIKLKGVDDR DAANLLTNCE IVVDSSQLPQ LEEGDYYWKD LMGCQVVTTE
     GYDLGKVVDM METGSNDVLV IKANLKDAFG IKERLVPFLD GQVIKKVDLT TRSIEVDWDP
     GF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025