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Database: UniProt
Entry: Q9RXK2
LinkDB: Q9RXK2
Original site: Q9RXK2 
ID   RL3_DEIRA               Reviewed;         211 AA.
AC   Q9RXK2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   18-SEP-2019, entry version 112.
DE   RecName: Full=50S ribosomal protein L3;
GN   Name=rplC; OrderedLocusNames=DR_0311;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, AND PROTEIN
RP   SEQUENCE OF 1-5.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA   Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA   Bartels H., Franceschi F., Yonath A.;
RT   "High resolution structure of the large ribosomal subunit from a
RT   mesophilic eubacterium.";
RL   Cell 107:679-688(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH FIVE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=11677599; DOI=10.1038/35101544;
RA   Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A.,
RA   Albrecht R., Yonath A., Franceschi F.;
RT   "Structural basis for the interaction of antibiotics with the peptidyl
RT   transferase centre in eubacteria.";
RL   Nature 413:814-821(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH TRNA MIMICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=12535524; DOI=10.1016/s1097-2765(03)00009-1;
RA   Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R.,
RA   Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E.,
RA   Kessler M., Yonath A.;
RT   "Structural basis of the ribosomal machinery for peptide bond
RT   formation, translocation, and nascent chain progression.";
RL   Mol. Cell 11:91-102(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH MODIFIED MACROLIDE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=12623020; DOI=10.1016/s0969-2126(03)00022-4;
RA   Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H.,
RA   Zarivach R., Yonath A.;
RT   "Structural basis for the antibiotic activity of ketolides and
RT   azalides.";
RL   Structure 11:329-338(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH TROLEANDOMYCIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=12665853; DOI=10.1038/nsb915;
RA   Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D.,
RA   Yonath A.;
RT   "Structural insight into the role of the ribosomal tunnel in cellular
RT   regulation.";
RL   Nat. Struct. Biol. 10:366-370(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=15059283; DOI=10.1186/1741-7007-2-4;
RA   Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.;
RT   "Alterations at the peptidyl transferase centre of the ribosome
RT   induced by the synergistic action of the streptogramins dalfopristin
RT   and quinupristin.";
RL   BMC Biol. 2:4-4(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX
RP   WITH TIAMULIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=15554968; DOI=10.1111/j.1365-2958.2004.04346.x;
RA   Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.;
RT   "Inhibition of peptide bond formation by pleuromutilins: the structure
RT   of the 50S ribosomal subunit from Deinococcus radiodurans in complex
RT   with tiamulin.";
RL   Mol. Microbiol. 54:1287-1294(2004).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly near the 3'-end of the 23S rRNA, where it nucleates
CC       assembly of the 50S subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. Also contacts proteins L13 and L17.
CC       {ECO:0000269|PubMed:11677599, ECO:0000269|PubMed:12535524,
CC       ECO:0000269|PubMed:12623020, ECO:0000269|PubMed:12665853,
CC       ECO:0000269|PubMed:15059283, ECO:0000269|PubMed:15554968}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000305}.
DR   EMBL; AE000513; AAF09892.1; -; Genomic_DNA.
DR   PIR; G75533; G75533.
DR   RefSeq; NP_294034.1; NC_001263.1.
DR   RefSeq; WP_010886956.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; B=1-211.
DR   PDB; 1NWX; X-ray; 3.50 A; B=1-211.
DR   PDB; 1NWY; X-ray; 3.30 A; B=1-211.
DR   PDB; 1SM1; X-ray; 3.42 A; B=1-211.
DR   PDB; 1XBP; X-ray; 3.50 A; B=1-211.
DR   PDB; 2OGM; X-ray; 3.50 A; B=1-211.
DR   PDB; 2OGN; X-ray; 3.56 A; B=1-211.
DR   PDB; 2OGO; X-ray; 3.66 A; B=1-211.
DR   PDB; 2ZJP; X-ray; 3.70 A; B=1-211.
DR   PDB; 2ZJQ; X-ray; 3.30 A; B=1-211.
DR   PDB; 2ZJR; X-ray; 2.91 A; B=1-211.
DR   PDB; 3CF5; X-ray; 3.30 A; B=1-211.
DR   PDB; 3DLL; X-ray; 3.50 A; B=1-211.
DR   PDB; 3PIO; X-ray; 3.25 A; B=1-211.
DR   PDB; 3PIP; X-ray; 3.45 A; B=1-211.
DR   PDB; 4IO9; X-ray; 3.20 A; B=1-211.
DR   PDB; 4IOA; X-ray; 3.20 A; B=1-211.
DR   PDB; 4IOC; X-ray; 3.60 A; B=1-211.
DR   PDB; 4U67; X-ray; 3.65 A; B=1-211.
DR   PDB; 4V49; X-ray; 8.70 A; B=1-205.
DR   PDB; 4V4A; X-ray; 9.50 A; B=1-205.
DR   PDB; 4V4G; X-ray; 11.50 A; E=1-205.
DR   PDB; 4WFN; X-ray; 3.54 A; B=1-211.
DR   PDB; 5DM6; X-ray; 2.90 A; B=1-205.
DR   PDB; 5DM7; X-ray; 3.00 A; B=1-205.
DR   PDB; 5JVG; X-ray; 3.43 A; B=1-211.
DR   PDB; 5JVH; X-ray; 3.58 A; B=1-211.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
DR   PDBsum; 1SM1; -.
DR   PDBsum; 1XBP; -.
DR   PDBsum; 2OGM; -.
DR   PDBsum; 2OGN; -.
DR   PDBsum; 2OGO; -.
DR   PDBsum; 2ZJP; -.
DR   PDBsum; 2ZJQ; -.
DR   PDBsum; 2ZJR; -.
DR   PDBsum; 3CF5; -.
DR   PDBsum; 3DLL; -.
DR   PDBsum; 3PIO; -.
DR   PDBsum; 3PIP; -.
DR   PDBsum; 4IO9; -.
DR   PDBsum; 4IOA; -.
DR   PDBsum; 4IOC; -.
DR   PDBsum; 4U67; -.
DR   PDBsum; 4V49; -.
DR   PDBsum; 4V4A; -.
DR   PDBsum; 4V4G; -.
DR   PDBsum; 4WFN; -.
DR   PDBsum; 5DM6; -.
DR   PDBsum; 5DM7; -.
DR   PDBsum; 5JVG; -.
DR   PDBsum; 5JVH; -.
DR   SMR; Q9RXK2; -.
DR   STRING; 243230.DR_0311; -.
DR   PRIDE; Q9RXK2; -.
DR   EnsemblBacteria; AAF09892; AAF09892; DR_0311.
DR   GeneID; 1799285; -.
DR   KEGG; dra:DR_0311; -.
DR   PATRIC; fig|243230.17.peg.477; -.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   InParanoid; Q9RXK2; -.
DR   KO; K02906; -.
DR   OMA; KGMRMAG; -.
DR   OrthoDB; 1270636at2; -.
DR   EvolutionaryTrace; Q9RXK2; -.
DR   Proteomes; UP000002524; Chromosome I.
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: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; Complete proteome; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1    211       50S ribosomal protein L3.
FT                                /FTId=PRO_0000077097.
FT   STRAND        3     16       {ECO:0000244|PDB:5DM6}.
FT   STRAND       19     27       {ECO:0000244|PDB:5DM6}.
FT   STRAND       35     37       {ECO:0000244|PDB:5DM6}.
FT   HELIX        39     42       {ECO:0000244|PDB:5DM6}.
FT   STRAND       46     50       {ECO:0000244|PDB:5DM6}.
FT   HELIX        56     58       {ECO:0000244|PDB:5DM6}.
FT   HELIX        61     69       {ECO:0000244|PDB:5DM6}.
FT   STRAND       78     83       {ECO:0000244|PDB:5DM6}.
FT   STRAND       87     90       {ECO:0000244|PDB:2ZJR}.
FT   HELIX        92     95       {ECO:0000244|PDB:5DM6}.
FT   STRAND      101    107       {ECO:0000244|PDB:5DM6}.
FT   STRAND      112    114       {ECO:0000244|PDB:5DM6}.
FT   HELIX       116    120       {ECO:0000244|PDB:5DM6}.
FT   STRAND      127    130       {ECO:0000244|PDB:5DM6}.
FT   STRAND      135    137       {ECO:0000244|PDB:5DM6}.
FT   STRAND      144    147       {ECO:0000244|PDB:4IOA}.
FT   STRAND      157    161       {ECO:0000244|PDB:5DM6}.
FT   STRAND      164    176       {ECO:0000244|PDB:5DM6}.
FT   TURN        177    180       {ECO:0000244|PDB:5DM6}.
FT   STRAND      181    186       {ECO:0000244|PDB:5DM6}.
FT   STRAND      194    199       {ECO:0000244|PDB:5DM6}.
SQ   SEQUENCE   211 AA;  22437 MW;  04D0EE53A6276CE4 CRC64;
     MKGILGTKIG MTQIWKNDRA IPVTVVLAGP CPIVQRKTAQ TDGYEAVQIG YAPKAERKVN
     KPMQGHFAKA GVAPTRILRE FRGFAPDGDS VNVDIFAEGE KIDATGTSKG KGTQGVMKRW
     NFAGGPASHG SKKWHRRPGS IGQRKTPGRV YKGKRMAGHM GMERVTVQNL EVVEIRAGEN
     LILVKGAIPG ANGGLVVLRS AAKASAAKGG K
//
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