ID   RL2_CARRP               Reviewed;         235 AA.
AC   Q05FI7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=50S ribosomal protein L2;
GN   Name=rplB; OrderedLocusNames=CRP_153;
OS   Carsonella ruddii (strain PV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=387662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV;
RX   PubMed=17038615; DOI=10.1126/science.1134196;
RA   Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA   Hattori M.;
RT   "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL   Science 314:267-267(2006).
CC   -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC       association of the 30S and 50S subunits to form the 70S ribosome, for
CC       tRNA binding and peptide bond formation. It has been suggested to have
CC       peptidyltransferase activity; this is somewhat controversial. Makes
CC       several contacts with the 16S rRNA in the 70S ribosome (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC       subunit in the 70S ribosome (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
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DR   EMBL; AP009180; BAF35184.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05FI7; -.
DR   SMR; Q05FI7; -.
DR   STRING; 387662.CRP_153; -.
DR   EnsemblBacteria; BAF35184; BAF35184; CRP_153.
DR   KEGG; crp:CRP_153; -.
DR   HOGENOM; CLU_036235_2_1_6; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000000777; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR022671; Ribosomal_L2_CS.
DR   InterPro; IPR014726; Ribosomal_L2_dom3.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR01171; rplB_bact; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..235
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000309893"
FT   REGION          197..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  26445 MW;  DE532AB3B062C2A9 CRC64;
     MKNKIKSLCL IKKKKSGRSR GKISVRHIGK KHKKFYRKID FKRDKYNIKG IVESIHYDPN
     RNARIALIKY LDGEKRYIIK TNNLEISNFV VSSLNKISLN SGNSTIIKNI NIGTLINCVE
     IFPKIGGIFS RSSGSESEII FKDNKFGVIK LPSGIKKKIS LNCMATIGKI CTFNVKKKLY
     KAGQNRWRGI RPTVRGVAMN PVDHPHGGGE GKTSGGRHPC SLWGIKTKGY KTKKK