ID   RL2_MYCCT               Reviewed;         281 AA.
AC   P10133; Q2SRF6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=MCAP_0693;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3481422; DOI=10.1007/bf00325700;
RA   Ohkubo S., Muto A., Kawauchi Y., Yamao F., Osawa S.;
RT   "The ribosomal protein gene cluster of Mycoplasma capricolum.";
RL   Mol. Gen. Genet. 210:314-322(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC       subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR   EMBL; X06414; CAA29707.1; -; Genomic_DNA.
DR   EMBL; CP000123; ABC01190.1; -; Genomic_DNA.
DR   PIR; S02834; R5YM2C.
DR   RefSeq; WP_011387542.1; NC_007633.1.
DR   AlphaFoldDB; P10133; -.
DR   SMR; P10133; -.
DR   EnsemblBacteria; ABC01190; ABC01190; MCAP_0693.
DR   GeneID; 23778353; -.
DR   KEGG; mcp:MCAP_0693; -.
DR   HOGENOM; CLU_036235_2_1_14; -.
DR   OMA; SCIELRP; -.
DR   OrthoDB; 961486at2; -.
DR   PhylomeDB; P10133; -.
DR   Proteomes; UP000001928; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   HAMAP; MF_01320_B; Ribosomal_L2_B; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..281
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129579"
FT   REGION          223..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="K -> N (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19..30
FT                   /note="IDYSAVLTTKNT -> TECSLFNNQKIA (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36..37
FT                   /note="VV -> GG (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="K -> T (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47..48
FT                   /note="NR -> KS (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..53
FT                   /note="TT -> SS (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="H -> Q (in Ref. 1; CAA29707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  31020 MW;  3D22E312F9E235C7 CRC64;
     MAIKKYKSTT NGRRNMTTID YSAVLTTKNT PEKSLVVSKS SKAGRNNRGL ITTRHKGGGH
     KQKYRIIDFK RNKRDIFGTI STIEYDPNRN AFICLVNYVD GEKRYILFAK GMQVGMKVVA
     SENADIKVGN SAPLKNIPEG TLLHNVELKP GKGGQIARSA GSSVQLLGKD DDGRYVTLRL
     SSGEVRKVLS ECYATIGEVG NEEYNLVNWG KAGRNRWRGI RPTVRGSVMN PNDHPHGGGE
     GRAPIGRKSP VTPWGKKALG VKTRNTKKAS EKLIVRKRSK K