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RL5_VIBPA
ID   RL5_VIBPA               Reviewed;         179 AA.
AC   Q87T01;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=VP0269;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58532.1; -; Genomic_DNA.
DR   RefSeq; NP_796648.1; NC_004603.1.
DR   RefSeq; WP_005455660.1; NC_004603.1.
DR   AlphaFoldDB; Q87T01; -.
DR   SMR; Q87T01; -.
DR   STRING; 223926.28805251; -.
DR   EnsemblBacteria; BAC58532; BAC58532; BAC58532.
DR   GeneID; 1187736; -.
DR   KEGG; vpa:VP0269; -.
DR   PATRIC; fig|223926.6.peg.260; -.
DR   eggNOG; COG0094; Bacteria.
DR   HOGENOM; CLU_061015_2_1_6; -.
DR   OMA; ERMYAFL; -.
DR   Proteomes; UP000002493; Chromosome 1.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..179
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000125023"
SQ   SEQUENCE   179 AA;  20130 MW;  6200E8C3AF04C48B CRC64;
     MAKLHDYYKS SVVAELTKQF SYTSVMQVPR IEKITLNMGV GEAINDKKLL ENAASDMATI
     SGQKPLITKA RKSVAGFKIR EGYPIGCKVT LRGERMWDFL ERLINIALPR VRDFRGVSAK
     SFDGRGNYSM GVREQIIFPE IDFDKVDRVR GLDITITTSA GTDEEGRALL AAFNFPFRK
 
 
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