RL23_STAAN
ID RL23_STAAN Reviewed; 91 AA.
AC Q7A459;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=SA2045;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC the proteins that surrounds the polypeptide exit tunnel on the outside
CC of the ribosome. Forms the main docking site for trigger factor binding
CC to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC trigger factor when it is bound to the ribosome. {ECO:0000255|HAMAP-
CC Rule:MF_01369}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR EMBL; BA000018; BAB43340.1; -; Genomic_DNA.
DR PIR; C90022; C90022.
DR RefSeq; WP_000388082.1; NC_002745.2.
DR AlphaFoldDB; Q7A459; -.
DR SMR; Q7A459; -.
DR EnsemblBacteria; BAB43340; BAB43340; BAB43340.
DR KEGG; sau:SA2045; -.
DR HOGENOM; CLU_037562_3_2_9; -.
DR OMA; FEVDHRA; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
PE 1: Evidence at protein level;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..91
FT /note="50S ribosomal protein L23"
FT /id="PRO_0000224172"
SQ SEQUENCE 91 AA; 10605 MW; A8F978ED9DE8092C CRC64;
MEARDILKRP VITEKSSEAM AEDKYTFDVD TRVNKTQVKM AVEEIFNVKV ASVNIMNYKP
KKKRMGRYQG YTNKRRKAIV TLKEGSIDLF N