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Database: UniProt
Entry: Q1AU31
LinkDB: Q1AU31
Original site: Q1AU31 
ID   RL23_RUBXD              Reviewed;          95 AA.
AC   Q1AU31;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   29-MAY-2013, entry version 46.
DE   RecName: Full=50S ribosomal protein L23;
GN   Name=rplW; OrderedLocusNames=Rxyl_2153;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129).
OC   Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales;
OC   Rubrobacterineae; Rubrobacteraceae; Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E.,
RA   Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG05097.1; -; Genomic_DNA.
DR   RefSeq; YP_644909.1; NC_008148.1.
DR   ProteinModelPortal; Q1AU31; -.
DR   STRING; 266117.Rxyl_2153; -.
DR   EnsemblBacteria; ABG05097; ABG05097; Rxyl_2153.
DR   GeneID; 4114807; -.
DR   KEGG; rxy:Rxyl_2153; -.
DR   PATRIC; 23371116; VBIRubXyl52678_2145.
DR   eggNOG; COG0089; -.
DR   HOGENOM; HOG000231366; -.
DR   KO; K02892; -.
DR   OMA; HRAAKPD; -.
DR   BioCyc; RXYL266117:GH8O-2192-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:HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA: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; L23_L15e_core; 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     95       50S ribosomal protein L23.
FT                                /FTId=PRO_0000272833.
SQ   SEQUENCE   95 AA;  10975 MW;  E038D5C1F5EF1EB5 CRC64;
     MDPHQIIIRP VISEKSYNLI ENEGQYTFEV DRRANKNQIK KAVEEAFDVK VKKVNTVNVK
     SKPKRQGFTR GRTSTWKKAV VKLAEGDRIE LFEGV
//
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