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Database: UniProt
Entry: Q9RY65
LinkDB: Q9RY65
Original site: Q9RY65 
ID   RL27_DEIRA              Reviewed;          91 AA.
AC   Q9RY65;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-OCT-2019, entry version 121.
DE   RecName: Full=50S ribosomal protein L27;
GN   Name=rpmA; OrderedLocusNames=DR_0085;
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: Binds the 5S and 23S rRNAs and also the tRNA in the P
CC       site.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L18.
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 bacterial ribosomal protein bL27
CC       family. {ECO:0000305}.
DR   EMBL; AE000513; AAF09678.1; -; Genomic_DNA.
DR   PIR; E75560; E75560.
DR   RefSeq; NP_293811.1; NC_001263.1.
DR   RefSeq; WP_010886733.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; U=1-91.
DR   PDB; 1NWX; X-ray; 3.50 A; U=1-91.
DR   PDB; 1NWY; X-ray; 3.30 A; U=1-91.
DR   PDB; 1SM1; X-ray; 3.42 A; U=1-91.
DR   PDB; 1XBP; X-ray; 3.50 A; U=1-91.
DR   PDB; 1Y69; X-ray; 3.33 A; U=1-91.
DR   PDB; 2ZJP; X-ray; 3.70 A; T=1-91.
DR   PDB; 2ZJQ; X-ray; 3.30 A; T=1-91.
DR   PDB; 2ZJR; X-ray; 2.91 A; T=1-91.
DR   PDB; 3CF5; X-ray; 3.30 A; T=1-91.
DR   PDB; 3DLL; X-ray; 3.50 A; T=1-91.
DR   PDB; 3PIO; X-ray; 3.25 A; T=1-91.
DR   PDB; 3PIP; X-ray; 3.45 A; T=1-91.
DR   PDB; 4IO9; X-ray; 3.20 A; T=1-91.
DR   PDB; 4IOA; X-ray; 3.20 A; T=1-91.
DR   PDB; 4IOC; X-ray; 3.60 A; T=1-91.
DR   PDB; 4U67; X-ray; 3.65 A; T=1-91.
DR   PDB; 4V49; X-ray; 8.70 A; U=2-87.
DR   PDB; 4V4A; X-ray; 9.50 A; U=2-87.
DR   PDB; 4V4G; X-ray; 11.50 A; X=2-87.
DR   PDB; 4V4T; X-ray; 6.46 A; 0=1-91.
DR   PDB; 4WFN; X-ray; 3.54 A; T=1-91.
DR   PDB; 5DM6; X-ray; 2.90 A; T=2-85.
DR   PDB; 5DM7; X-ray; 3.00 A; T=2-85.
DR   PDB; 5JVG; X-ray; 3.43 A; T=1-91.
DR   PDB; 5JVH; X-ray; 3.58 A; T=1-91.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
DR   PDBsum; 1SM1; -.
DR   PDBsum; 1XBP; -.
DR   PDBsum; 1Y69; -.
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; 4V4T; -.
DR   PDBsum; 4WFN; -.
DR   PDBsum; 5DM6; -.
DR   PDBsum; 5DM7; -.
DR   PDBsum; 5JVG; -.
DR   PDBsum; 5JVH; -.
DR   SMR; Q9RY65; -.
DR   STRING; 243230.DR_0085; -.
DR   PRIDE; Q9RY65; -.
DR   EnsemblBacteria; AAF09678; AAF09678; DR_0085.
DR   GeneID; 1799586; -.
DR   KEGG; dra:DR_0085; -.
DR   PATRIC; fig|243230.17.peg.249; -.
DR   eggNOG; ENOG4105K46; Bacteria.
DR   eggNOG; COG0211; LUCA.
DR   HOGENOM; HOG000111610; -.
DR   InParanoid; Q9RY65; -.
DR   KO; K02899; -.
DR   OMA; GKDHTLH; -.
DR   OrthoDB; 1904463at2; -.
DR   EvolutionaryTrace; Q9RY65; -.
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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   DisProt; DP00886; -.
DR   HAMAP; MF_00539; Ribosomal_L27; 1.
DR   InterPro; IPR001684; Ribosomal_L27.
DR   InterPro; IPR018261; Ribosomal_L27_CS.
DR   PANTHER; PTHR15893; PTHR15893; 1.
DR   Pfam; PF01016; Ribosomal_L27; 1.
DR   PRINTS; PR00063; RIBOSOMALL27.
DR   TIGRFAMs; TIGR00062; L27; 1.
DR   PROSITE; PS00831; RIBOSOMAL_L27; 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; tRNA-binding.
FT   CHAIN         1     91       50S ribosomal protein L27.
FT                                /FTId=PRO_0000181082.
FT   STRAND       22     25       {ECO:0000244|PDB:5DM6}.
FT   STRAND       27     29       {ECO:0000244|PDB:1Y69}.
FT   STRAND       36     39       {ECO:0000244|PDB:5DM6}.
FT   STRAND       41     47       {ECO:0000244|PDB:5DM6}.
FT   STRAND       51     53       {ECO:0000244|PDB:5DM6}.
FT   STRAND       59     63       {ECO:0000244|PDB:5DM6}.
FT   STRAND       66     71       {ECO:0000244|PDB:5DM6}.
FT   STRAND       73     75       {ECO:0000244|PDB:5DM6}.
FT   STRAND       77     82       {ECO:0000244|PDB:5DM6}.
SQ   SEQUENCE   91 AA;  9590 MW;  BF3CDBA77E9DC47C CRC64;
     MAHKKGVGSS KNGRDSNPKY LGVKKFGGEV VKAGNILVRQ RGTKFKAGQG VGMGRDHTLF
     ALSDGKVVFI NKGKGARFIS IEAAQTEVAA D
//
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