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RL30_DEIRA
ID   RL30_DEIRA              Reviewed;          55 AA.
AC   Q9RSL0;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371};
GN   Name=rpmD {ECO:0000255|HAMAP-Rule:MF_01371}; OrderedLocusNames=DR_2114;
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   PROTEIN SEQUENCE OF 1-5, AND X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE
RP   50S SUBUNIT.
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: Binds the 5S and 23S rRNAs.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01371, ECO:0000269|PubMed:11677599,
CC       ECO:0000269|PubMed:12535524, ECO:0000269|PubMed:12623020,
CC       ECO:0000269|PubMed:12665853, ECO:0000269|PubMed:15059283,
CC       ECO:0000269|PubMed:15554968}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01371}.
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DR   EMBL; AE000513; AAF11663.1; -; Genomic_DNA.
DR   PIR; E75314; E75314.
DR   RefSeq; NP_295837.1; NC_001263.1.
DR   RefSeq; WP_010888745.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; X=1-55.
DR   PDB; 1NWX; X-ray; 3.50 A; X=1-55.
DR   PDB; 1NWY; X-ray; 3.30 A; X=1-55.
DR   PDB; 1SM1; X-ray; 3.42 A; X=1-55.
DR   PDB; 1XBP; X-ray; 3.50 A; X=1-55.
DR   PDB; 2ZJP; X-ray; 3.70 A; W=1-55.
DR   PDB; 2ZJQ; X-ray; 3.30 A; W=1-55.
DR   PDB; 2ZJR; X-ray; 2.91 A; W=1-55.
DR   PDB; 3CF5; X-ray; 3.30 A; W=1-55.
DR   PDB; 3DLL; X-ray; 3.50 A; W=1-55.
DR   PDB; 3PIO; X-ray; 3.25 A; W=1-55.
DR   PDB; 3PIP; X-ray; 3.45 A; W=1-55.
DR   PDB; 4IO9; X-ray; 3.20 A; W=1-55.
DR   PDB; 4IOA; X-ray; 3.20 A; W=1-55.
DR   PDB; 4IOC; X-ray; 3.60 A; W=1-55.
DR   PDB; 4U67; X-ray; 3.65 A; W=1-55.
DR   PDB; 4V49; X-ray; 8.70 A; X=1-55.
DR   PDB; 4V4A; X-ray; 9.50 A; X=1-55.
DR   PDB; 4V4G; X-ray; 11.50 A; Z=1-55.
DR   PDB; 4WFN; X-ray; 3.54 A; W=1-55.
DR   PDB; 5DM6; X-ray; 2.90 A; W=1-55.
DR   PDB; 5DM7; X-ray; 3.00 A; W=1-55.
DR   PDB; 5JVG; X-ray; 3.43 A; W=1-55.
DR   PDB; 5JVH; X-ray; 3.58 A; W=1-55.
DR   PDB; 7A0R; X-ray; 3.30 A; W=1-55.
DR   PDB; 7A0S; X-ray; 3.22 A; W=1-55.
DR   PDB; 7A18; X-ray; 3.40 A; W=1-55.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
DR   PDBsum; 1SM1; -.
DR   PDBsum; 1XBP; -.
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; Q9RSL0; -.
DR   SMR; Q9RSL0; -.
DR   IntAct; Q9RSL0; 1.
DR   STRING; 243230.DR_2114; -.
DR   EnsemblBacteria; AAF11663; AAF11663; DR_2114.
DR   GeneID; 59163716; -.
DR   KEGG; dra:DR_2114; -.
DR   PATRIC; fig|243230.17.peg.2337; -.
DR   eggNOG; COG1841; Bacteria.
DR   HOGENOM; CLU_131047_2_1_0; -.
DR   InParanoid; Q9RSL0; -.
DR   OMA; GKQNQRD; -.
DR   OrthoDB; 2084745at2; -.
DR   EvolutionaryTrace; Q9RSL0; -.
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-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01658; Ribosomal_L30; 1.
DR   Gene3D; 3.30.1390.20; -; 1.
DR   HAMAP; MF_01371_B; Ribosomal_L30_B; 1.
DR   InterPro; IPR036919; L30_ferredoxin-like_sf.
DR   InterPro; IPR005996; Ribosomal_L30_bac-type.
DR   InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR   PANTHER; PTHR15892; PTHR15892; 1.
DR   Pfam; PF00327; Ribosomal_L30; 1.
DR   PIRSF; PIRSF002211; Ribosomal_L30_bac-type; 1.
DR   SUPFAM; SSF55129; SSF55129; 1.
DR   TIGRFAMs; TIGR01308; rpmD_bact; 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..55
FT                   /note="50S ribosomal protein L30"
FT                   /id="PRO_0000104589"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           14..22
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:5DM6"
SQ   SEQUENCE   55 AA;  6067 MW;  F3592EF664026A56 CRC64;
     MKIKLVRSVI GRPGNQVKTV QALGLRKIGD SREVSDTPAV RGMVKTVKHL LEVQE
 
 
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