GenomeNet

Database: UniProt
Entry: P42920
LinkDB: P42920
Original site: P42920 
ID   RL3_BACSU               Reviewed;         209 AA.
AC   P42920;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   29-SEP-2021, entry version 122.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
DE            Short=BL3;
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=BSU01160;
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=SG38;
RX   PubMed=9371452; DOI=10.1128/jb.179.22.7046-7054.1997;
RA   Li X., Lindahl L., Sha Y., Zengel J.M.;
RT   "Analysis of the Bacillus subtilis S10 ribosomal protein gene cluster
RT   identifies two promoters that may be responsible for transcription of the
RT   entire 15-kilobase S10-spc-alpha cluster.";
RL   J. Bacteriol. 179:7046-7054(1997).
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   FUNCTION IN STIMULATING RRNA PROCESSING BY MRNC (MINI-RIBONUCLEASE 3).
RX   PubMed=19154332; DOI=10.1111/j.1365-2958.2008.06591.x;
RA   Redko Y., Condon C.;
RT   "Ribosomal protein L3 bound to 23S precursor rRNA stimulates its maturation
RT   by Mini-III ribonuclease.";
RL   Mol. Microbiol. 71:1145-1154(2009).
RN   [5]
RP   INTERACTION WITH CSHA, AND SUBUNIT.
RC   STRAIN=168;
RX   PubMed=23175651; DOI=10.1128/jb.01475-12;
RA   Lehnik-Habrink M., Rempeters L., Kovacs A.T., Wrede C., Baierlein C.,
RA   Krebber H., Kuipers O.P., Stulke J.;
RT   "DEAD-box RNA helicases in Bacillus subtilis have multiple functions and
RT   act independently from each other.";
RL   J. Bacteriol. 195:534-544(2013).
RN   [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-209 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: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit (By similarity). Strongly stimulates 23S rRNA precursor
CC       processing by mini-ribonuclease 3 (MrnC); 20-30% DMSO can replace L3,
CC       suggesting the protein may alter rRNA conformation. {ECO:0000255|HAMAP-
CC       Rule:MF_01325, ECO:0000269|PubMed:19154332}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:30126986). Forms a
CC       cluster with proteins L14 and L19 (By similarity). Interacts with RNA
CC       helicase CshA (PubMed:23175651). {ECO:0000255|HAMAP-Rule:MF_01325,
CC       ECO:0000269|PubMed:23175651, ECO:0000269|PubMed:30126986}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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; U43929; AAC45956.1; -; Genomic_DNA.
DR   EMBL; D50302; BAA08831.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11892.1; -; Genomic_DNA.
DR   EMBL; D64127; BAA11007.1; -; Genomic_DNA.
DR   PIR; G69694; G69694.
DR   RefSeq; NP_387997.1; NC_000964.3.
DR   RefSeq; WP_004399671.1; NZ_JNCM01000029.1.
DR   PDB; 3J3V; EM; 13.30 A; D=1-209.
DR   PDB; 3J3W; EM; 10.70 A; D=1-209.
DR   PDB; 3J9W; EM; 3.90 A; BE=1-209.
DR   PDB; 5NJT; EM; 3.80 A; X=2-208.
DR   PDB; 6HA1; EM; 3.10 A; D=1-209.
DR   PDB; 6HA8; EM; 3.50 A; D=1-209.
DR   PDB; 6HTQ; EM; 4.50 A; D=2-207.
DR   PDB; 6PPF; EM; 3.40 A; D=1-209.
DR   PDB; 6PPK; EM; 4.40 A; D=1-209.
DR   PDB; 6PVK; EM; 3.40 A; D=1-209.
DR   PDB; 6TNN; EM; 3.07 A; X=1-209.
DR   PDB; 6TPQ; EM; 3.07 A; X=1-209.
DR   PDB; 7AQC; EM; 2.99 A; D=1-209.
DR   PDB; 7AQD; EM; 3.10 A; D=1-209.
DR   PDB; 7AS8; EM; 2.90 A; F=1-209.
DR   PDB; 7AS9; EM; 3.50 A; F=1-209.
DR   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   PDBsum; 6HTQ; -.
DR   PDBsum; 6PPF; -.
DR   PDBsum; 6PPK; -.
DR   PDBsum; 6PVK; -.
DR   PDBsum; 6TNN; -.
DR   PDBsum; 6TPQ; -.
DR   PDBsum; 7AQC; -.
DR   PDBsum; 7AQD; -.
DR   PDBsum; 7AS8; -.
DR   PDBsum; 7AS9; -.
DR   SMR; P42920; -.
DR   IntAct; P42920; 1.
DR   STRING; 224308.BSU01160; -.
DR   jPOST; P42920; -.
DR   PaxDb; P42920; -.
DR   PRIDE; P42920; -.
DR   EnsemblBacteria; CAB11892; CAB11892; BSU_01160.
DR   GeneID; 936239; -.
DR   KEGG; bsu:BSU01160; -.
DR   PATRIC; fig|224308.179.peg.119; -.
DR   eggNOG; COG0087; Bacteria.
DR   InParanoid; P42920; -.
DR   OMA; GKNIPCT; -.
DR   PhylomeDB; P42920; -.
DR   BioCyc; BSUB:BSU01160-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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; IBA:GO_Central.
DR   GO; GO:2000234; P:positive regulation of rRNA processing; IDA:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03625; L3_bact; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA processing; rRNA-binding.
FT   CHAIN           1..209
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077066"
FT   REGION          122..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          4..14
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           63..70
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          78..86
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:7AQC"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          107..113
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   HELIX           122..126
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:7AS9"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   TURN            181..184
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:7AS8"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:7AS8"
SQ   SEQUENCE   209 AA;  22683 MW;  44A0FDF6F3C681AB CRC64;
     MTKGILGRKI GMTQVFAENG DLIPVTVIEA APNVVLQKKT AENDGYEAIQ LGFDDKREKL
     SNKPEKGHVA KAETAPKRFV KELRGVEMDA YEVGQEVKVE IFSAGEIVDV TGVSKGKGFQ
     GAIKRHGQSR GPMSHGSRYH RRPGSMGPVD PNRVFKGKLL PGRMGGEQIT VQNLEIVKVD
     AERNLLLIKG NVPGAKKSLI TVKSAVKSK
//
DBGET integrated database retrieval system