ID   RL2_METH1               Reviewed;         281 AA.
AC   Q8GM57; D1J883;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=MHO_2950;
OS   Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC
OS   10111 / PG21) (Mycoplasma hominis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=347256;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12234836; DOI=10.1128/aac.46.10.3142-3150.2002;
RA   Pereyre S., Gonzalez P., De Barbeyrac B., Darnige A., Renaudin H.,
RA   Charron A., Raherison S., Bebear C., Bebear C.M.;
RT   "Mutations in 23S rRNA account for intrinsic resistance to macrolides in
RT   Mycoplasma hominis and Mycoplasma fermentans and for acquired resistance to
RT   macrolides in M. hominis.";
RL   Antimicrob. Agents Chemother. 46:3142-3150(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC 10111 / PG21;
RX   PubMed=19816563; DOI=10.1371/journal.pgen.1000677;
RA   Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A.,
RA   Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A.,
RA   Bebear C.;
RT   "Life on arginine for Mycoplasma hominis: clues from its minimal genome and
RT   comparison with other human urogenital mycoplasmas.";
RL   PLoS Genet. 5:E1000677-E1000677(2009).
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; AY083306; AAM08938.1; -; Genomic_DNA.
DR   EMBL; FP236530; CAX37430.1; -; Genomic_DNA.
DR   RefSeq; WP_012855571.1; NC_013511.1.
DR   AlphaFoldDB; Q8GM57; -.
DR   SMR; Q8GM57; -.
DR   STRING; 347256.MHO_2950; -.
DR   EnsemblBacteria; CAX37430; CAX37430; MHO_2950.
DR   GeneID; 57139972; -.
DR   KEGG; mho:MHO_2950; -.
DR   eggNOG; COG0090; Bacteria.
DR   HOGENOM; CLU_036235_2_1_14; -.
DR   OMA; SCIELRP; -.
DR   OrthoDB; 961486at2; -.
DR   Proteomes; UP000002631; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..281
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129582"
FT   REGION          222..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31018 MW;  0831B8132A2C92FB CRC64;
     MAIKKFKAYT NGRRNMSSLD YQANLTGHAP EKSLLVALPT KAGRNNQGKI TTRHQGGRLK
     RFYRIIDFKR QKDGIPATVK TIEYDPNRSA NISLVVYRDG EKRYILSPKG IKIGQVILSG
     DNVDIQVGNH LPLANIPEGT FVHNIELQPR QGGIIARSAG SSAQILGKDE SGRYVILRLK
     SGEVRKVLAI NRATVGEVGN EEHSLVNIGK AGRNRLRGIR PTVRGSAMNP NDHPHGGGEG
     RQPIGRKSPM TPWGKRALGV KTRATKKASN QFIIRRRKET K