RL2_ACTPJ
ID RL2_ACTPJ Reviewed; 273 AA.
AC B0BST4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-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=APJL_1798;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(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; CP000687; ABY70348.1; -; Genomic_DNA.
DR RefSeq; WP_005599291.1; NC_010278.1.
DR AlphaFoldDB; B0BST4; -.
DR SMR; B0BST4; -.
DR EnsemblBacteria; ABY70348; ABY70348; APJL_1798.
DR GeneID; 66258525; -.
DR KEGG; apj:APJL_1798; -.
DR HOGENOM; CLU_036235_2_1_6; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000008547; 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..273
FT /note="50S ribosomal protein L2"
FT /id="PRO_1000141496"
FT REGION 31..50
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 254..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 29894 MW; 2B7850B8D793C80E CRC64;
MAIVKCKPTS AGRRHVVKVV NAELHKGKPY APLLDSKSKT GGRNNLGRIT TRHIGGGHKQ
HYRLVDFKRN KLDIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL SVGDTIQAGV
SAPIKAGNAL PMRNIPVGTT VHNVELKPGK GGQIARSAGA YVQIIAREGN YVTLRLRSGE
MRKVLAECTA TIGEVGNSEH MLRVLGKAGA NRWRGVRPTV RGTAMNPVDH PHGGGEGRNF
GKHPVTPWGV QTKGKKTRHN KRTDKYIVRR RGK