RL23_SYNS3
ID RL23_SYNS3 Reviewed; 100 AA.
AC Q0ID07;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
GN Synonyms=rpl23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN OrderedLocusNames=sync_0435;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000435; ABI46523.1; -; Genomic_DNA.
DR RefSeq; WP_011618397.1; NC_008319.1.
DR AlphaFoldDB; Q0ID07; -.
DR SMR; Q0ID07; -.
DR STRING; 64471.sync_0435; -.
DR EnsemblBacteria; ABI46523; ABI46523; sync_0435.
DR KEGG; syg:sync_0435; -.
DR eggNOG; COG0089; Bacteria.
DR HOGENOM; CLU_037562_3_2_3; -.
DR OMA; FEVDHRA; -.
DR OrthoDB; 1978865at2; -.
DR Proteomes; UP000001961; 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; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..100
FT /note="50S ribosomal protein L23"
FT /id="PRO_0000272856"
SQ SEQUENCE 100 AA; 11351 MW; FBDD699484EF1ECC CRC64;
MTERFTGRLA DVIRRPLITE KATRALEQNQ YTFEVDHRAA KPDIKAAVEQ LFDVKVTGIS
TMNPPRRSRR IGRFAGKRAQ VKKAVVRLAE GNSIQLFPES