ID   RL2_SPIKU               Reviewed;         278 AA.
AC   P60404;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
OS   Spiroplasma kunkelii.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=47834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CR2-3x;
RX   PubMed=12845528; DOI=10.1007/s00438-003-0878-3;
RA   Zhao Y., Hammond R.W., Jomantiene R., Dally E.L., Lee I.-M., Jia H., Wu H.,
RA   Lin S., Zhang P., Kenton S., Najar F.Z., Hua A., Roe B.A., Fletcher J.,
RA   Davis R.E.;
RT   "Gene content and organization of an 85-kb DNA segment from the genome of
RT   the phytopathogenic mollicute Spiroplasma kunkelii.";
RL   Mol. Genet. Genomics 269:592-602(2003).
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; AY198133; AAP58895.1; -; Genomic_DNA.
DR   AlphaFoldDB; P60404; -.
DR   SMR; P60404; -.
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..278
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129613"
FT   REGION          223..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..278
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  30847 MW;  03A77FFE387A1798 CRC64;
     MPIKSFKPVT PSRRNMTSLD YSVLTTDRPE KSLIKTRKKH AGRNNQGVIT TRHKGGGHKV
     KYRIIDFKRN KDNIIGKIAT IEYDPNRNAF ICLVNYVDGE KRYILAPKTI KVGMQIVSAE
     KTDIKVGNCM KLKNIPEGTV LHNLELRPGK GGQLARSAGS SVQFLGKDED GKYVTIRLTS
     GEVRKVLGEC RATVGEVGNE DYALVNWGKA GRNRWRGIRP TVRGSAMNPN DHPHGGGEGK
     APVGRKAPMT PWGKKALGVK TRNKKKASTK LIVRRRTK