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Database: UniProt
Entry: P46899
LinkDB: P46899
Original site: P46899 
ID   RL18_BACSU              Reviewed;         120 AA.
AC   P46899; P70969;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-SEP-2021, entry version 127.
DE   RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337};
DE   AltName: Full=BL16;
GN   Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; OrderedLocusNames=BSU01320;
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 / 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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA   Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA   Kawamura F., Yoshikawa H., Takahashi H.;
RT   "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT   subtilis chromosome.";
RL   Microbiology 142:3039-3046(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]
RP   SEQUENCE REVISION TO 37.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION IN RNASE M5 CLEAVAGE, RRNA-BINDING, AND SUBUNIT.
RX   PubMed=6432797;
RA   Stahl D.A., Pace B., Marsh T., Pace N.R.;
RT   "The ribonucleoprotein substrate for a ribosomal RNA-processing nuclease.";
RL   J. Biol. Chem. 259:11448-11453(1984).
RN   [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-120 WITH AND WITHOUT
RP   VIRGINIAMYCIN M.
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 one 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. {ECO:0000255|HAMAP-
CC       Rule:MF_01337}.
CC   -!- FUNCTION: Required for correct processing of both the 5' and 3' ends of
CC       5S rRNA precursor, which is does in conjunction with ribonuclease M5
CC       (RNase M5, rnmV). Possibly folds the 5S rRNA precursor into the correct
CC       conformation, thus acting as a chaperone. {ECO:0000269|PubMed:6432797}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:30126986). Part of
CC       the 5S rRNA/L5/L18/L25 subcomplex (Probable). Contacts the 23S rRNA and
CC       5S rRNA (Probable). Required for catalysis of RNase M5
CC       (PubMed:6432797). {ECO:0000269|PubMed:30126986,
CC       ECO:0000269|PubMed:6432797, ECO:0000305|PubMed:6432797}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01337}.
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DR   EMBL; L47971; AAB06815.1; -; Genomic_DNA.
DR   EMBL; D64125; BAA10982.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11908.2; -; Genomic_DNA.
DR   PIR; D69696; D69696.
DR   RefSeq; NP_388013.2; NC_000964.3.
DR   RefSeq; WP_003225816.1; NZ_JNCM01000029.1.
DR   PDB; 3J3V; EM; 13.30 A; O=1-120.
DR   PDB; 3J9W; EM; 3.90 A; BR=1-120.
DR   PDB; 5NJT; EM; 3.80 A; h=1-120.
DR   PDB; 6HA1; EM; 3.10 A; O=1-120.
DR   PDB; 6HA8; EM; 3.50 A; O=1-120.
DR   PDB; 6HTQ; EM; 4.50 A; O=1-120.
DR   PDB; 6PPF; EM; 3.40 A; O=1-120.
DR   PDB; 6PPK; EM; 4.40 A; O=1-120.
DR   PDB; 6TNN; EM; 3.07 A; h=1-120.
DR   PDB; 6TPQ; EM; 3.07 A; h=1-120.
DR   PDB; 7AQC; EM; 2.99 A; O=1-120.
DR   PDB; 7AQD; EM; 3.10 A; O=1-120.
DR   PDB; 7AS8; EM; 2.90 A; S=1-120.
DR   PDB; 7AS9; EM; 3.50 A; S=1-120.
DR   PDBsum; 3J3V; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   PDBsum; 6HTQ; -.
DR   PDBsum; 6PPF; -.
DR   PDBsum; 6PPK; -.
DR   PDBsum; 6TNN; -.
DR   PDBsum; 6TPQ; -.
DR   PDBsum; 7AQC; -.
DR   PDBsum; 7AQD; -.
DR   PDBsum; 7AS8; -.
DR   PDBsum; 7AS9; -.
DR   SMR; P46899; -.
DR   STRING; 224308.BSU01320; -.
DR   jPOST; P46899; -.
DR   PaxDb; P46899; -.
DR   PRIDE; P46899; -.
DR   EnsemblBacteria; CAB11908; CAB11908; BSU_01320.
DR   GeneID; 64301970; -.
DR   GeneID; 936785; -.
DR   KEGG; bsu:BSU01320; -.
DR   PATRIC; fig|224308.179.peg.135; -.
DR   eggNOG; COG0256; Bacteria.
DR   InParanoid; P46899; -.
DR   OMA; NKQIYAQ; -.
DR   PhylomeDB; P46899; -.
DR   BioCyc; BSUB:BSU01320-MONOMER; -.
DR   SABIO-RK; P46899; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR   InterPro; IPR005484; Ribosomal_L18.
DR   InterPro; IPR004389; Ribosomal_L18_bac-type.
DR   PANTHER; PTHR12899; PTHR12899; 1.
DR   Pfam; PF00861; Ribosomal_L18p; 1.
DR   TIGRFAMs; TIGR00060; L18_bact; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA processing; rRNA-binding.
FT   CHAIN           1..120
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_0000131216"
FT   CONFLICT        37
FT                   /note="N -> Y (in Ref. 2; BAA10982)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..19
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:6TPQ"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           71..87
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:7AS9"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           105..116
FT                   /evidence="ECO:0007829|PDB:7AS8"
SQ   SEQUENCE   120 AA;  12969 MW;  20DC3DEF58B2A8FF CRC64;
     MITKTSKNAA RLKRHARVRA KLSGTAERPR LNVFRSNKHI YAQIIDDVNG VTLASASTLD
     KDLNVESTGD TSAATKVGEL VAKRAAEKGI SDVVFDRGGY LYHGRVKALA DAAREAGLKF
//
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