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Database: UniProt
Entry: Q1J912
LinkDB: Q1J912
Original site: Q1J912 
ID   RL23_STRPF              Reviewed;          98 AA.
AC   Q1J912;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   01-OCT-2014, entry version 58.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=MGAS10750_Spy0049;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29,
CC       and trigger factor when it is bound to the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR   EMBL; CP000262; ABF36999.1; -; Genomic_DNA.
DR   RefSeq; YP_601543.1; NC_008024.1.
DR   ProteinModelPortal; Q1J912; -.
DR   STRING; 370554.MGAS10750_Spy0049; -.
DR   EnsemblBacteria; ABF36999; ABF36999; MGAS10750_Spy0049.
DR   GeneID; 4067353; -.
DR   KEGG; spi:MGAS10750_Spy0049; -.
DR   PATRIC; 19726252; VBIStrPyo25933_0049.
DR   eggNOG; COG0089; -.
DR   HOGENOM; HOG000231366; -.
DR   KO; K02892; -.
DR   OMA; TAGMMND; -.
DR   OrthoDB; EOG6HTP4P; -.
DR   BioCyc; SPYO370554:GI3S-81-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_1000068169.
SQ   SEQUENCE   98 AA;  10732 MW;  C3CDA22DE967D8EC CRC64;
     MNLYDVIKKP VITEKSMIAL EAGKYTFEVD TRAHKLLIKQ AVEAAFDGVK VASVNTVNVK
     PKAKRVGRYT GFTSKTKKAI ITLTADSKAI ELFAAEAE
//
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