RL2_SYNPW
ID RL2_SYNPW Reviewed; 287 AA.
AC A5GIU2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
GN Synonyms=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN OrderedLocusNames=SynWH7803_0431;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-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; CT971583; CAK22857.1; -; Genomic_DNA.
DR RefSeq; WP_011932345.1; NC_009481.1.
DR AlphaFoldDB; A5GIU2; -.
DR SMR; A5GIU2; -.
DR STRING; 32051.SynWH7803_0431; -.
DR EnsemblBacteria; CAK22857; CAK22857; SynWH7803_0431.
DR KEGG; syx:SynWH7803_0431; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_3; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000001566; Chromosome.
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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..287
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000310033"
FT REGION 221..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31625 MW; 65E2E9786D53DA23 CRC64;
MAIRSFRPYT PGTRTRVVTD FSEVTGRKPE RSLVVSKHRR KGRNNRGVIT CRHRGGGHKR
QYRVVDFRRN KHGVPAKVAA IHYDPHRNAR LALLFYTDGE KRYILAPAGV TVGQTVISGP
DAPIEDGNAM PLSSVPLGSS VHCVELYAGR GGQMVRTAGA SAQVMAKEGD YVALKLPSTE
VRLVRRECYA TLGEVGNSEI RNTSLGKAGR RRWLGRRPQV RGSVMNPCDH PHGGGEGRAP
IGRSGPVTPW GKPALGLKTR KRNKPSNKFV LRKRRKTSKR SRGGRDS
