ID   RL2_ASTYP               Reviewed;         276 AA.
AC   Q50264;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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};
GN   Synonyms=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320};
OS   Aster yellows phytoplasma.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=35779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1769558; DOI=10.1016/0378-1097(91)90397-s;
RA   Lim P.O., Sears B.B.;
RT   "DNA sequence of the ribosomal protein genes rpl2 and rps19 from a plant-
RT   pathogenic mycoplasma-like organism.";
RL   FEMS Microbiol. Lett. 68:71-73(1991).
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; M74770; AAA25327.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50264; -.
DR   SMR; Q50264; -.
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..276
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129524"
FT   REGION          221..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  30396 MW;  71563029AEA64620 CRC64;
     MAIKKYKPTT NGCRNMSVSA FSEITTQTPE KRLLVSHKDQ AGRNNQGKIT VRHRGGGVKR
     KYRLIDFKRN KDNIVGKVAT IEYDPNRSAN IALIHYLDGE KRYILAPKGL TVGMQIVSGK
     EADIKVANCL SLMNIPVGTT VHNIELKPGK GGQIARSAGS FCQIISREDK YVLLRLQSGE
     VPKVLGTCRA TIGEIGNESY KLINYGKAGK KRFLGIRPTV RGSAMNPNDH PHGGGEGRAP
     IGRKSPMTPW GKKARGVKTR DRKKASNALI IRRRTK