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Database: UniProt
Entry: P12877
LinkDB: P12877
Original site: P12877 
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   29-SEP-2021, entry version 139.
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   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   SMR; P12877; -.
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-MONOMER; -.
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
//
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