RL3_BACSU
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 03-AUG-2022, entry version 125.
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}.
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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 PDB; 7O5B; EM; 3.33 A; a=1-208.
DR PDB; 7OPE; EM; 3.20 A; F=1-209.
DR PDB; 7QV1; EM; 3.50 A; D=1-209.
DR PDB; 7QV2; EM; 3.50 A; D=1-209.
DR PDB; 7QV3; EM; 5.14 A; D=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 PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P42920; -.
DR SMR; P42920; -.
DR IntAct; P42920; 2.
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; KRMAGRY; -.
DR PhylomeDB; P42920; -.
DR BioCyc; BSUB:BSU01160-MON; -.
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
