ID   RL5_RHOPA               Reviewed;         185 AA.
AC   Q6N4U5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
DE   AltName: Full=RRP-L5;
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=RPA3238;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   MASS SPECTROMETRY.
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=15473684; DOI=10.1021/pr049940z;
RA   Strader M.B., VerBerkmoes N.C., Tabb D.L., Connelly H.M., Barton J.W.,
RA   Bruce B.D., Pelletier D.A., Davison B.H., Hettich R.L., Larimer F.W.,
RA   Hurst G.B.;
RT   "Characterization of the 70S ribosome from Rhodopseudomonas palustris using
RT   an integrated 'top-down' and 'bottom-up' mass spectrometric approach.";
RL   J. Proteome Res. 3:965-978(2004).
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 rRNA
CC       subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to
CC       the 30S subunit in the 70S ribosome (By similarity). {ECO:0000250}.
CC   -!- PTM: Both N-terminus methionine truncation and retention have been
CC       observed for this protein.
CC   -!- PTM: May be methylated twice, on undetermined residues.
CC   -!- MASS SPECTROMETRY: Mass=21064.6; Method=Electrospray; Note=For the
CC       protein without N-terminus methionine removal.;
CC       Evidence={ECO:0000269|PubMed:15473684};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
CC   -!- CAUTION: Both N-terminus methionine truncation and retention have been
CC       observed for this protein by 2 different experiments. {ECO:0000305}.
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DR   EMBL; BX572603; CAE28679.1; -; Genomic_DNA.
DR   RefSeq; WP_011158783.1; NC_005296.1.
DR   AlphaFoldDB; Q6N4U5; -.
DR   SMR; Q6N4U5; -.
DR   IntAct; Q6N4U5; 1.
DR   STRING; 258594.RPA3238; -.
DR   PRIDE; Q6N4U5; -.
DR   EnsemblBacteria; CAE28679; CAE28679; RPA3238.
DR   GeneID; 66894324; -.
DR   KEGG; rpa:RPA3238; -.
DR   eggNOG; COG0094; Bacteria.
DR   HOGENOM; CLU_061015_2_1_5; -.
DR   OMA; ERMYAFL; -.
DR   PhylomeDB; Q6N4U5; -.
DR   BioCyc; RPAL258594:TX73_RS16520-MON; -.
DR   Proteomes; UP000001426; 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   1: Evidence at protein level;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..185
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000124977"
SQ   SEQUENCE   185 AA;  21038 MW;  A9A6DCA21992DBF4 CRC64;
     MAETAYVPRL RTEYDRHIRT QLTEKFGYAN VMQVPKLDKV VLNMGVGEAV NDRKKAEQAA
     ADLSLIAGQK AVITYSRVAI STFKLRENQP IGCKVTLRQA RMYEFIDRLI TVALPRVRDF
     RGLNPKSFDG RGNYSLGIKE HIIFPEIDFD KTGESWGMDI TVCTTARTDD EARALLTAFN
     FPFRQ