RL5_SHIF8
ID RL5_SHIF8 Reviewed; 179 AA.
AC Q0SZZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=SFV_3328;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: This is 1 of the proteins that binds and probably mediates
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. In the 70S ribosome it contacts
CC protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC this bridge is implicated in subunit movement. Contacts the P site
CC tRNA; the 5S rRNA and some of its associated proteins might help
CC stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01333}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA.
CC Forms a bridge to the 30S subunit in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR EMBL; CP000266; ABF05371.1; -; Genomic_DNA.
DR RefSeq; WP_001096200.1; NC_008258.1.
DR AlphaFoldDB; Q0SZZ4; -.
DR SMR; Q0SZZ4; -.
DR EnsemblBacteria; ABF05371; ABF05371; SFV_3328.
DR GeneID; 64293237; -.
DR GeneID; 67415349; -.
DR KEGG; sfv:SFV_3328; -.
DR HOGENOM; CLU_061015_2_1_6; -.
DR OMA; ERMYAFL; -.
DR BioCyc; SFLE373384:SFV_RS18345-MON; -.
DR Proteomes; UP000000659; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1440.10; -; 1.
DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR020930; Ribosomal_L5_bac-type.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 3: Inferred from homology;
KW Acetylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..179
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000052830"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01333"
SQ SEQUENCE 179 AA; 20302 MW; B2E95A8BE4B8D2A7 CRC64;
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL DNAAADLAAI
SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF ERLITIAVPR IRDFRGLSAK
SFDGRGNYSM GVREQIIFPE IDYDKVDRVR GLDITITTTA KSDEEGRALL AAFDFPFRK
