RL2_GRAFK
ID RL2_GRAFK Reviewed; 279 AA.
AC A0M595;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, 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}; OrderedLocusNames=GFO_2836;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67790.1; -; Genomic_DNA.
DR RefSeq; WP_011710693.1; NC_008571.1.
DR AlphaFoldDB; A0M595; -.
DR SMR; A0M595; -.
DR STRING; 411154.GFO_2836; -.
DR EnsemblBacteria; CAL67790; CAL67790; GFO_2836.
DR KEGG; gfo:GFO_2836; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_10; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000000755; 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; 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.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..279
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000309924"
FT REGION 223..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30460 MW; E182C98F34B45A22 CRC64;
MSVRKLKPIT PGQRFRVVNG YDAITTDKPE KSLLAPIKKS GGRNSQGKMT MRYKGGGHKK
RYRVIDFKRD KQGIPATVAS IEYDPNRTAF IALLNYQDGE KRYIIAQNGL QVDQNVVSSN
EAATPEIGNA MPLANIPLGT VISCIELRPG QGAVMARSAG AFAQLLAREG KYATIKLPSG
EIRRVLALCM ATIGAVSNSD HQLMIGGKAG RSRWLGIRPR TRPVAMNPVD HPMGGGEGRA
SGGHPRSRKG LPAKGFKTRS RTKASNKYIV ERRKTRKKK