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RL2_SALG2
ID   RL2_SALG2               Reviewed;         273 AA.
AC   B5RH18;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=SG4002;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR39772.1; -; Genomic_DNA.
DR   RefSeq; WP_000301869.1; NC_011274.1.
DR   AlphaFoldDB; B5RH18; -.
DR   SMR; B5RH18; -.
DR   EnsemblBacteria; CAR39772; CAR39772; SG4002.
DR   GeneID; 64338586; -.
DR   GeneID; 67515078; -.
DR   KEGG; seg:SG4002; -.
DR   HOGENOM; CLU_036235_2_1_6; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000008321; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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..273
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_1000141609"
FT   REGION          28..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..273
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  29820 MW;  771CDD297EC65137 CRC64;
     MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLVEKNSKS GGRNNNGRIT TRHIGGGHKQ
     AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL KAGDQIQSGV
     DAAIKAGNTL PMRNIPVGST VHNVEMKPGK GGQLARSAGT YVQIVARDGA YVTLRLRSGE
     MRKVEADCRA TLGEVGNAEH MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF
     GKHPVTPWGV QTKGKKTRSN KRTDKFIVRR RSK
 
 
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