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Database: UniProt
Entry: C0M6X1
LinkDB: C0M6X1
Original site: C0M6X1 
ID   RL23_STRE4              Reviewed;          98 AA.
AC   C0M6X1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   19-FEB-2014, entry version 30.
DE   RecName: Full=50S ribosomal protein L23;
GN   Name=rplW; OrderedLocusNames=SEQ_0057;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K.,
RA   Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K.,
RA   Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K.,
RA   Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M.,
RA   Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J.,
RA   Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA.
CC       One of the proteins that surrounds the polypeptide exit tunnel on
CC       the outside of the ribosome. Forms the main docking site for
CC       trigger factor binding to the ribosome (By similarity).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29,
CC       and trigger factor when it is bound to the ribosome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR   EMBL; FM204883; CAW91971.1; -; Genomic_DNA.
DR   RefSeq; YP_002745485.1; NC_012471.1.
DR   STRING; 553482.SEQ_0057; -.
DR   EnsemblBacteria; CAW91971; CAW91971; SEQ_0057.
DR   GeneID; 7697472; -.
DR   KEGG; seu:SEQ_0057; -.
DR   PATRIC; 19644821; VBIStrEqu13040_0055.
DR   eggNOG; COG0089; -.
DR   HOGENOM; HOG000231366; -.
DR   KO; K02892; -.
DR   OMA; TAGMMND; -.
DR   OrthoDB; EOG6HTP4P; -.
DR   ProtClustDB; PRK05738; -.
DR   BioCyc; SEQU553482:GJOY-76-MONOMER; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1     98       50S ribosomal protein L23.
FT                                /FTId=PRO_1000184105.
SQ   SEQUENCE   98 AA;  10868 MW;  C4CAD52F56C1CCE9 CRC64;
     MNLYDVIKKP VITEKSMYAL EEGKYTFEVD TRAHKLLIKQ AVEAAFDGVK VASVNTVNVK
     PKAKRVGRYT GFTSKTKKAI ITLTADSKAI ELFAVEAE
//
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