RL2_SYNP2
ID RL2_SYNP2 Reviewed; 275 AA.
AC B1XJT6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SYNPCC7002_A1062;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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; CP000951; ACA99064.1; -; Genomic_DNA.
DR RefSeq; WP_012306687.1; NC_010475.1.
DR AlphaFoldDB; B1XJT6; -.
DR SMR; B1XJT6; -.
DR STRING; 32049.SYNPCC7002_A1062; -.
DR EnsemblBacteria; ACA99064; ACA99064; SYNPCC7002_A1062.
DR KEGG; syp:SYNPCC7002_A1062; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_3; -.
DR OMA; SCIELRP; -.
DR Proteomes; UP000001688; 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..275
FT /note="50S ribosomal protein L2"
FT /id="PRO_1000141627"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30628 MW; 858C265324208E3E CRC64;
MGIRSFRPYT PGTRQATVSD FSEITKSKPE KSLTKYKHRK KGRNNRGVIT CRHRGGGHKR
LYRLIDFRRD KRDITAQVTA IEYDPNRNAR IALVQYEDGE KRYILQPAGL GVGDTIIAGE
EAPYEIGNAL PLYKIPLGTE IHNIELYAGR GGQMVRSAGA FAQLVAKEGD YVTIKLPSKE
VRMVRKECYA TIGKVGNAEA RNLKLGKAGR TRHLGRRPQV RGSVMNPVDH PHGGGEGRAP
IGRSGPVTPW GKPALGKKTR KKKKQSSSLI VRRRR
