ID   RL2_STRCU               Reviewed;         278 AA.
AC   Q9AMK8;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
OS   Streptomyces collinus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=42684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 5-26; 32-40;
RP   53-88; 92-154; 158-188; 191-208; 214-239; 245-252 AND 267-270.
RX   PubMed=11478805; DOI=10.1006/bbrc.2001.5336;
RA   Mikulik K., Man P., Halada P.;
RT   "Characterization of the rplB gene from Streptomyces collinus and its
RT   protein product by mass spectrometry.";
RL   Biochem. Biophys. Res. Commun. 285:1344-1349(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 15-26; 92-102 AND 135-154, AND PHOSPHORYLATION.
RX   PubMed=9299515; DOI=10.1006/bbrc.1997.7297;
RA   Mikulik K., Janda I.;
RT   "Protein kinase associated with ribosomes phosphorylates ribosomal proteins
RT   of Streptomyces collinus.";
RL   Biochem. Biophys. Res. Commun. 238:370-376(1997).
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   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {ECO:0000269|PubMed:9299515}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR   EMBL; AF324467; AAK01662.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AMK8; -.
DR   SMR; Q9AMK8; -.
DR   GO; GO:0015934; C:large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..278
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129626"
FT   REGION          29..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..278
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        154
FT                   /note="K -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  30493 MW;  35B739F55850A395 CRC64;
     MAIRKYKPTT PGRRGASVAD FVEVTRSTPE KSLVRPLHSK GGRNNAGRIT VRHQGGGHKR
     AYRIVDFRRH DKDGVPAKVA HIEYDPNRSA RIALLHYADG EKRYILAPRN LQQGDRVENG
     PGADIKPGNN LALRNIPVGT TIHAIELRPG GGAKFARSAG ASVQLLAKEG AYAHLRMPSG
     EIRLVNVRCR ATIGEVGNAE QSNINWGKAG RKRWLGVRPT VRGVVMNPVD HPHGGGEGRT
     SGGRHPVSPW GKPTGRTRSN KKASNKYIVR RRTKNKKR