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Database: UniProt
Entry: Q6GEI5
LinkDB: Q6GEI5
Original site: Q6GEI5 
ID   RL23_STAAR              Reviewed;          91 AA.
AC   Q6GEI5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   14-MAY-2014, entry version 69.
DE   RecName: Full=50S ribosomal protein L23;
GN   Name=rplW; OrderedLocusNames=SAR2333;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41314.1; -; Genomic_DNA.
DR   RefSeq; YP_041688.1; NC_002952.2.
DR   ProteinModelPortal; Q6GEI5; -.
DR   SMR; Q6GEI5; 2-89.
DR   STRING; 282458.SAR2333; -.
DR   EnsemblBacteria; CAG41314; CAG41314; SAR2333.
DR   GeneID; 2860918; -.
DR   KEGG; sar:SAR2333; -.
DR   PATRIC; 19548337; VBIStaAur71814_2345.
DR   eggNOG; COG0089; -.
DR   HOGENOM; HOG000231366; -.
DR   KO; K02892; -.
DR   OMA; GKTKRMG; -.
DR   OrthoDB; EOG6HTP4P; -.
DR   BioCyc; SAUR282458:GJA5-2376-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; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1     91       50S ribosomal protein L23.
FT                                /FTId=PRO_0000224173.
SQ   SEQUENCE   91 AA;  10605 MW;  A8F978ED9DE8092C CRC64;
     MEARDILKRP VITEKSSEAM AEDKYTFDVD TRVNKTQVKM AVEEIFNVKV ASVNIMNYKP
     KKKRMGRYQG YTNKRRKAIV TLKEGSIDLF N
//
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