RL2_MYCAP
ID RL2_MYCAP Reviewed; 281 AA.
AC A5IYY3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=MAG5430;
OS Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS agalactiae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=347257;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA Blanchard A., Citti C.;
RT "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT bacterial genome.";
RL PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59242.1; -; Genomic_DNA.
DR RefSeq; WP_011949702.1; NC_009497.1.
DR AlphaFoldDB; A5IYY3; -.
DR SMR; A5IYY3; -.
DR STRING; 347257.MAG5430; -.
DR EnsemblBacteria; CAL59242; CAL59242; MAG5430.
DR KEGG; maa:MAG5430; -.
DR HOGENOM; CLU_036235_2_1_14; -.
DR OMA; SCIELRP; -.
DR Proteomes; UP000007065; 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_1000141584"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 30678 MW; 5602483A1C71FA6F CRC64;
MAVKHYKPVT NGRRNMSSLD YSKNLSGHAP EKSLLVILKK NSGRNNQGKI TVRHQGGRVK
RYYRIIDFKR NKDDIPATVK SIEYDPNRSA NICLLAYADG EKRYILAPEG IKVGQKVVSG
NNVDILVGNS LPLSNIPEGT FVHNVEMQPG GGGIIARSAG TSAQILGKDD DGKYVVLRLK
SGEMRRILAR CRATIGTVGN GEHSLVLLGK AGRSRHLGVR PTVRGSVMNP IDHPHGGGVS
KQPIGRKAPL TPWGKKALGV KTRKTKKSST KLILRRRKDS K