(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 114.
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).
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. Forms a cluster with
CC       proteins L14 and L19 (By similarity). Interacts with RNA helicase CshA.
CC       {ECO:0000255|HAMAP-Rule:MF_01325, ECO:0000269|PubMed:23175651}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   SMR; P42920; -.
DR   IntAct; P42920; 1.
DR   STRING; 224308.BSU01160; -.
DR   jPOST; P42920; -.
DR   PaxDb; P42920; -.
DR   PRIDE; P42920; -.
DR   EnsemblBacteria; CAB11892; CAB11892; BSU01160.
DR   GeneID; 936239; -.
DR   KEGG; bsu:BSU01160; -.
DR   PATRIC; fig|224308.179.peg.119; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   InParanoid; P42920; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   PhylomeDB; P42920; -.
DR   BioCyc; BSUB:BSU01160-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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;
DR   PRODOM; P42920.
DR   SWISS-2DPAGE; P42920.
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"
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
//

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