ID   RL5_AYWBP               Reviewed;         181 AA.
AC   Q2NIW6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=AYWB_510;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYWB;
RX   PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA   Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to diverse
RT   environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65627.1; -; Genomic_DNA.
DR   RefSeq; WP_011412789.1; NC_007716.1.
DR   AlphaFoldDB; Q2NIW6; -.
DR   SMR; Q2NIW6; -.
DR   STRING; 322098.AYWB_510; -.
DR   EnsemblBacteria; ABC65627; ABC65627; AYWB_510.
DR   KEGG; ayw:AYWB_510; -.
DR   eggNOG; COG0094; Bacteria.
DR   HOGENOM; CLU_061015_2_1_14; -.
DR   OMA; ERMYAFL; -.
DR   PhylomeDB; Q2NIW6; -.
DR   Proteomes; UP000001934; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..181
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000242963"
SQ   SEQUENCE   181 AA;  20311 MW;  85CE981AB5976466 CRC64;
     MSIKKENTLD YSKITATLMK TFNYKSVMQV PKVDKVVINM GVGDAIFNVK VLDDVVEELK
     LLSGQSPVIT KAKKAISNFK LREGMPIGAK VTLRGARKEA FLYKLTRLVL PRVRDFRGIS
     GKSFDGRGNY ALGLKEQIVF PEINIDKVKK IRGMDIIIVT TAKNNTQAKK LLELYGMPFK
     N