ID RL5_BACSU Reviewed; 179 AA. AC P12877; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 02-SEP-2026, entry version 161. DE RecName: Full=Large ribosomal subunit protein uL5 {ECO:0000255|HAMAP-Rule:MF_01333}; DE AltName: Full=50S ribosomal protein L5 {ECO:0000305}; DE AltName: Full=BL6; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=BSU01280; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=2508062; DOI=10.1093/nar/17.18.7469; RA Henkin T.M., Moon S.H., Mattheakis L.C., Nomura M.; RT "Cloning and analysis of the spc ribosomal protein operon of Bacillus RT subtilis: comparison with the spc operon of Escherichia coli."; RL Nucleic Acids Res. 17:7469-7486(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / RC NCIMB 3610 / NRRL NRS-744 / VKM B-501; RX PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1; RA Suh J.-W., Boylan S.A., Oh S.H., Price C.W.; RT "Genetic and transcriptional organization of the Bacillus subtilis spc- RT alpha region."; RL Gene 169:17-23(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-179 WITH AND WITHOUT RP VIRGINIAMYCIN M, INTERACTION WITH VMLR, AND SUBUNIT. RX PubMed=30126986; DOI=10.1073/pnas.1808535115; RA Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M., RA Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.; RT "Structural basis for antibiotic resistance mediated by the Bacillus RT subtilis ABCF ATPase VmlR."; RL Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018). RN [5] {ECO:0007744|PDB:7QV3} RP STRUCTURE BY ELECTRON MICROSCOPY (5.14 ANGSTROMS) OF 70S RIBOSOME, AND RP INTERACTION WITH MUTS2. RC STRAIN=168; RX PubMed=35264791; DOI=10.1038/s41586-022-04487-6; RA Cerullo F., Filbeck S., Patil P.R., Hung H.C., Xu H., Vornberger J., RA Hofer F.W., Schmitt J., Kramer G., Bukau B., Hofmann K., Pfeffer S., RA Joazeiro C.A.P.; RT "Bacterial ribosome collision sensing by a MutS DNA repair ATPase RT paralogue."; RL Nature 603:509-514(2022). CC -!- FUNCTION: This is one of the proteins that bind and probably mediate 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 (PubMed:30126986). Part of CC the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site CC tRNA. Forms a bridge to the 30S subunit in the 70S ribosome (By CC similarity). Interacts with VmlR (PubMed:30126986). In stalled CC ribosomes contacts MutS2 (PubMed:35264791). {ECO:0000255|HAMAP- CC Rule:MF_01333, ECO:0000269|PubMed:30126986, CC ECO:0000269|PubMed:35264791}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X15664; CAA33703.1; -; Genomic_DNA. DR EMBL; L47971; AAB06811.1; -; Genomic_DNA. DR EMBL; AL009126; CAB11904.1; -; Genomic_DNA. DR PIR; S05994; R5BS5. DR RefSeq; NP_388009.1; NC_000964.3. DR RefSeq; WP_003225809.1; NC_000964.3. DR PDB; 3J3V; EM; 13.30 A; F=1-179. DR PDB; 3J9W; EM; 3.90 A; BG=1-179. DR PDB; 5NJT; EM; 3.80 A; Z=2-179. DR PDB; 6HA1; EM; 3.10 A; F=1-179. DR PDB; 6HA8; EM; 3.50 A; F=1-179. DR PDB; 6HTQ; EM; 4.50 A; F=2-177. DR PDB; 6PPK; EM; 4.40 A; F=1-179. DR PDB; 6TNN; EM; 3.07 A; Z=1-179. DR PDB; 6TPQ; EM; 3.07 A; Z=1-179. DR PDB; 7AQC; EM; 2.99 A; F=1-179. DR PDB; 7AQD; EM; 3.10 A; F=1-179. DR PDB; 7AS8; EM; 2.90 A; H=1-179. DR PDB; 7AS9; EM; 3.50 A; H=1-179. DR PDB; 7O5B; EM; 3.33 A; c=1-179. DR PDB; 7OPE; EM; 3.20 A; H=1-179. DR PDB; 7QGU; EM; 4.75 A; F=1-179. DR PDB; 7QH4; EM; 5.45 A; F=1-179. DR PDB; 7QV1; EM; 3.50 A; F=1-179. DR PDB; 7QV2; EM; 3.50 A; F=1-179. DR PDB; 7QV3; EM; 5.14 A; F=1-179. DR PDB; 8BUU; EM; 2.90 A; F=1-179. DR PDB; 8QCQ; EM; 2.30 A; F=1-179. DR PDB; 8QPP; EM; 3.40 A; c=2-179. DR PDB; 8R55; EM; 3.57 A; c=2-179. DR PDB; 8S1P; EM; 1.96 A; F=1-179. DR PDB; 8S1U; EM; 3.40 A; F=1-179. DR PDB; 9FY1; EM; 2.30 A; F=1-179. DR PDB; 9FY2; EM; 2.30 A; F=1-179. DR PDB; 9FY3; EM; 2.80 A; F=1-179. DR AlphaFoldDB; P12877; -. DR EMDB; EMD-0176; -. DR EMDB; EMD-0177; -. DR EMDB; EMD-0270; -. DR EMDB; EMD-10535; -. DR EMDB; EMD-10543; -. DR EMDB; EMD-11862; -. DR EMDB; EMD-11864; -. DR EMDB; EMD-11889; -. DR EMDB; EMD-11890; -. DR EMDB; EMD-12734; -. DR EMDB; EMD-13017; -. DR EMDB; EMD-14157; -. DR EMDB; EMD-14158; -. DR EMDB; EMD-14159; -. DR EMDB; EMD-16246; -. DR EMDB; EMD-18332; -. DR EMDB; EMD-19638; -. DR EMDB; EMD-19641; -. DR EMDB; EMD-3656; -. DR EMDB; EMD-50855; -. DR EMDB; EMD-50856; -. DR EMDB; EMD-50858; -. DR SMR; P12877; -. DR FunCoup; P12877; 689. DR IntAct; P12877; 1. DR STRING; 224308.BSU01280; -. DR jPOST; P12877; -. DR PaxDb; 224308-BSU01280; -. DR EnsemblBacteria; CAB11904; CAB11904; BSU_01280. DR GeneID; 306025514; -. DR GeneID; 86875474; -. DR GeneID; 936981; -. DR KEGG; bsu:BSU01280; -. DR PATRIC; fig|224308.179.peg.131; -. DR eggNOG; COG0094; Bacteria. DR InParanoid; P12877; -. DR OrthoDB; 9806626at2; -. DR PhylomeDB; P12877; -. DR BioCyc; BSUB:BSU01280-MONOMER; -. DR EvolutionaryTrace; P12877; -. DR PRO; PR:P12877; -. DR Proteomes; UP000001570; Chromosome. DR AbasyAtlas; P12877; -. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. 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; IBA:GO_Central. DR FunFam; 3.30.1440.10:FF:000001; 50S ribosomal protein L5; 1. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01333_B; Ribosomal_uL5_B; 1. DR InterPro; IPR002132; Ribosomal_uL5. DR InterPro; IPR020930; Ribosomal_uL5_bact. DR InterPro; IPR031309; Ribosomal_uL5_C. DR InterPro; IPR020929; Ribosomal_uL5_CS. DR InterPro; IPR022803; Ribosomal_uL5_dom_sf. DR InterPro; IPR031310; Ribosomal_uL5_N. DR NCBIfam; NF000585; PRK00010.1; 1. DR PANTHER; PTHR11994; 60S RIBOSOMAL PROTEIN L11-RELATED; 1. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; RL5-like; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. DR PDBsum; 3J3V; -. DR PDBsum; 3J9W; -. DR PDBsum; 5NJT; -. DR PDBsum; 6HA1; -. DR PDBsum; 6HA8; -. DR PDBsum; 6HTQ; -. DR PDBsum; 6PPK; -. DR PDBsum; 6TNN; -. DR PDBsum; 6TPQ; -. DR PDBsum; 7AQC; -. DR PDBsum; 7AQD; -. DR PDBsum; 7AS8; -. DR PDBsum; 7AS9; -. DR PDBsum; 7O5B; -. DR PDBsum; 7OPE; -. DR PDBsum; 7QGU; -. DR PDBsum; 7QH4; -. DR PDBsum; 7QV1; -. DR PDBsum; 7QV2; -. DR PDBsum; 7QV3; -. DR PDBsum; 8BUU; -. DR PDBsum; 8QCQ; -. DR PDBsum; 8QPP; -. DR PDBsum; 8R55; -. DR PDBsum; 8S1P; -. DR PDBsum; 8S1U; -. DR PDBsum; 9FY1; -. DR PDBsum; 9FY2; -. DR PDBsum; 9FY3; -. PE 1: Evidence at protein level; KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1..179 FT /note="Large ribosomal subunit protein uL5" FT /id="PRO_0000124892" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 8..12 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 13..20 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:7AQC" FT STRAND 31..39 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 41..44 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 47..61 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:7AS8" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:7AS8" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 103..107 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:7AQC" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:7O5B" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:6HA1" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:8S1P" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:8S1P" FT HELIX 163..173 FT /evidence="ECO:0007829|PDB:8S1P" SQ SEQUENCE 179 AA; 20148 MW; 57576598B0A7979B CRC64; MNRLKEKYNK EIAPALMTKF NYDSVMQVPK IEKIVINMGV GDAVQNAKAI DSAVEELTFI AGQKPVVTRA KKSIAGFRLR EGMPIGAKVT LRGERMYDFL DKLISVSLPR VRDFRGVSKK SFDGRGNYTL GIKEQLIFPE IDYDKVTKVR GMDIVIVTTA NTDEEARELL TQVGMPFQK //