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   27-MAR-2024, entry version 129.
DE   RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000305};
DE   AltName: Full=50S ribosomal protein L3;
GN   Name=rplC; OrderedLocusNames=DR_0311;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 radiodurans
RT   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 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 mesophilic
RT   eubacterium.";
RL   Cell 107:679-688(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   FIVE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=11677599; DOI=10.1038/35101544;
RA   Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R.,
RA   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 WITH
RP   TRNA MIMICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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., Kessler M.,
RA   Yonath A.;
RT   "Structural basis of the ribosomal machinery for peptide bond formation,
RT   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 WITH
RP   MODIFIED MACROLIDE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 azalides.";
RL   Structure 11:329-338(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TROLEANDOMYCIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 WITH
RP   THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 induced by
RT   the synergistic action of the streptogramins dalfopristin and
RT   quinupristin.";
RL   BMC Biol. 2:4-4(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TIAMULIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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 of
RT   the 50S ribosomal subunit from Deinococcus radiodurans in complex with
RT   tiamulin.";
RL   Mol. Microbiol. 54:1287-1294(2004).
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. {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}.
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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_JMLF01000001.1.
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   PDB; 7A0R; X-ray; 3.30 A; B=1-206.
DR   PDB; 7A0S; X-ray; 3.22 A; B=1-206.
DR   PDB; 7A18; X-ray; 3.40 A; B=1-206.
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   PDBsum; 7A0R; -.
DR   PDBsum; 7A0S; -.
DR   PDBsum; 7A18; -.
DR   AlphaFoldDB; Q9RXK2; -.
DR   SMR; Q9RXK2; -.
DR   IntAct; Q9RXK2; 1.
DR   STRING; 243230.DR_0311; -.
DR   PaxDb; 243230-DR_0311; -.
DR   EnsemblBacteria; AAF09892; AAF09892; DR_0311.
DR   GeneID; 69516543; -.
DR   KEGG; dra:DR_0311; -.
DR   PATRIC; fig|243230.17.peg.477; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_4_1_0; -.
DR   InParanoid; Q9RXK2; -.
DR   OrthoDB; 9806135at2; -.
DR   EvolutionaryTrace; Q9RXK2; -.
DR   Proteomes; UP000002524; Chromosome I.
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   Gene3D; 3.30.160.810; -; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_01325_B; Ribosomal_uL3_B; 1.
DR   InterPro; IPR000597; Ribosomal_uL3.
DR   InterPro; IPR019927; Ribosomal_uL3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_uL3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR03625; L3_bact; 1.
DR   PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..211
FT                   /note="Large ribosomal subunit protein uL3"
FT                   /id="PRO_0000077097"
FT   REGION          125..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..148
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          3..16
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          19..27
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          46..50
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           61..69
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           116..120
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:4IOA"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          164..176
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|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
//