RL3_DEIRA
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 25-MAY-2022, entry version 121.
DE RecName: Full=50S ribosomal protein L3;
GN Name=rplC; OrderedLocusNames=DR_0311;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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., 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 WITH
RP THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 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 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_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 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 EnsemblBacteria; AAF09892; AAF09892; DR_0311.
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 OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
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 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; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..211
FT /note="50S ribosomal protein L3"
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
