ID   A2SLF5_METPP            Unreviewed;       104 AA.
AC   A2SLF5;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Large ribosomal subunit protein uL23 {ECO:0000256|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000256|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=Mpe_A3441 {ECO:0000313|EMBL:ABM96394.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96394.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM96394.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000256|ARBA:ARBA00006700, ECO:0000256|HAMAP-Rule:MF_01369}.
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DR   EMBL; CP000555; ABM96394.1; -; Genomic_DNA.
DR   RefSeq; WP_011831015.1; NC_008825.1.
DR   AlphaFoldDB; A2SLF5; -.
DR   STRING; 420662.Mpe_A3441; -.
DR   KEGG; mpt:Mpe_A3441; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_3_1_4; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; IPR013025; Ribosomal_uL23-like.
DR   InterPro; IPR012678; Ribosomal_uL23/eL15/eS24_sf.
DR   PANTHER; PTHR11620; 60S RIBOSOMAL PROTEIN L23A; 1.
DR   PANTHER; PTHR11620:SF2; RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; Ribosomal proteins S24e, L23 and L15e; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01369};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01369};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01369};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01369}.
SQ   SEQUENCE   104 AA;  11347 MW;  5A878427767D6387 CRC64;
     MSALKFDEGR LMKVLVAPIV SEKATAVAES HNQVLFKVLQ DATKPEIKAA VELLFKVEVD
     KVSVVNTKGK TKRFGKGVGR RDNVRKAYVC LKAGQELNFS GEAA
//