RL5_BACSU
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 03-AUG-2022, entry version 142.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
DE AltName: Full=BL6;
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=BSU01280;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 / NCIMB
RC 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).
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 (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). {ECO:0000255|HAMAP-
CC Rule:MF_01333, ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
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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; NZ_JNCM01000029.1.
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; 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 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; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P12877; -.
DR SMR; P12877; -.
DR IntAct; P12877; 1.
DR STRING; 224308.BSU01280; -.
DR jPOST; P12877; -.
DR PaxDb; P12877; -.
DR PRIDE; P12877; -.
DR EnsemblBacteria; CAB11904; CAB11904; BSU_01280.
DR GeneID; 64301966; -.
DR GeneID; 936981; -.
DR KEGG; bsu:BSU01280; -.
DR PATRIC; fig|224308.179.peg.131; -.
DR eggNOG; COG0094; Bacteria.
DR InParanoid; P12877; -.
DR OMA; ERMYAFL; -.
DR PhylomeDB; P12877; -.
DR BioCyc; BSUB:BSU01280-MON; -.
DR PRO; PR:P12877; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..179
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000124892"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:7AS8"
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
