ID   RL2_FRATM               Reviewed;         274 AA.
AC   B2SDY2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=FTM_1524;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(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; CP000915; ACD31346.1; -; Genomic_DNA.
DR   RefSeq; WP_012429820.1; NC_010677.1.
DR   AlphaFoldDB; B2SDY2; -.
DR   SMR; B2SDY2; -.
DR   KEGG; ftm:FTM_1524; -.
DR   HOGENOM; CLU_036235_2_1_6; -.
DR   OMA; SCIELRP; -.
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..274
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_1000141556"
FT   REGION          224..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..274
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  30373 MW;  9527A2476F671E48 CRC64;
     MIEIKKAKPT SPGRRHVVSV KNTELHTGKP FKGLVEVKKS KAGRNNTGRI TVRHQGGGHK
     QHYRVVDFKR NKDDITAKVE RIEYDPNRSA NIALVLYADG ERRYIVAPKG LKKDMSVISG
     EKVDVAVGNC MPLRNIPLGT VIHNIEMKPK KGAQMIRSAG TFAQLVGKDN AYAIIRLRSG
     EMRRVLLDCR AVIGVVSNSE HNLKSLGKAG AKRWRGIRPT VRGVAMNPVD HPHGGGEGRT
     SGGRHPVTPW GIPTKGYKTR RNKRSNKLIV QKRK