ID   RL2_FRATH               Reviewed;         274 AA.
AC   Q2A5G7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=FTL_0239;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVS;
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AM233362; CAJ78680.1; -; Genomic_DNA.
DR   RefSeq; WP_011457354.1; NZ_CP009694.1.
DR   AlphaFoldDB; Q2A5G7; -.
DR   SMR; Q2A5G7; -.
DR   KEGG; ftl:FTL_0239; -.
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_0000309917"
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;  30401 MW;  7531C602CD46E732 CRC64;
     MIEIKKAKPT SPGRRHVVSV KNTELHTGKP FKGLVEVKKS KAGRNNTGRI TVRHQGGGHK
     QHYRIVDFKR NKDDITAKVE RIEYDPNRSA NIALVLYADG ERRYIVAPKG LKKDMSVISG
     EKVDIAVGNC MPLRNIPLGT VIHNIEMKPK KGAQMIRSAG TFAQLVGKDN AYAIIRLRSG
     EMRRVLLDCR AVIGVVSNSE HNLKSLGKAG AKRWRGIRPT VRGVAMNPVD HPHGGGEGRT
     SGGRHPVTPW GIPTKGYKTR RNKRSNKLIV QKRK