(data stored in ACNUC30630 zone)

SWISSPROT: RL24_DEIRA

ID   RL24_DEIRA              Reviewed;         115 AA.
AC   Q9RXJ1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=50S ribosomal protein L24;
GN   Name=rplX; OrderedLocusNames=DR_0322;
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).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TRIGGER FACTOR.
RX   PubMed=16271892; DOI=10.1016/j.str.2005.08.007;
RA   Schluenzen F., Wilson D.N., Tian P., Harms J.M., McInnes S.J.,
RA   Hansen H.A.S., Albrecht R., Buerger J., Wilbanks S.M., Fucini P.;
RT   "The binding mode of the trigger factor on the ribosome: implications for
RT   protein folding and SRP interaction.";
RL   Structure 13:1685-1694(2005).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000250}.
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. Contacts trigger factor (TF) when
CC       it is bound to the ribosome; this contact may expose a hydrophobic
CC       crevice in TF (PubMed:16271892). {ECO:0000269|PubMed:16271892}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts trigger factor
CC       when it is bound to the ribosome (PubMed:16271892).
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       ECO:0000269|PubMed:16271892}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000305}.
DR   EMBL; AE000513; AAF09903.1; -; Genomic_DNA.
DR   PIR; B75535; B75535.
DR   RefSeq; NP_294045.1; NC_001263.1.
DR   RefSeq; WP_010886967.1; NZ_CP015081.1.
DR   PDB; 1GS2; Model; -; S=2-115.
DR   PDB; 1NKW; X-ray; 3.10 A; S=1-115.
DR   PDB; 1NWX; X-ray; 3.50 A; S=1-115.
DR   PDB; 1NWY; X-ray; 3.30 A; S=1-115.
DR   PDB; 1SM1; X-ray; 3.42 A; S=1-115.
DR   PDB; 1XBP; X-ray; 3.50 A; S=1-115.
DR   PDB; 2D3O; X-ray; 3.35 A; S=1-115.
DR   PDB; 2ZJP; X-ray; 3.70 A; R=1-115.
DR   PDB; 2ZJQ; X-ray; 3.30 A; R=1-115.
DR   PDB; 2ZJR; X-ray; 2.91 A; R=1-115.
DR   PDB; 3CF5; X-ray; 3.30 A; R=1-115.
DR   PDB; 3DLL; X-ray; 3.50 A; R=1-115.
DR   PDB; 3PIO; X-ray; 3.25 A; R=1-115.
DR   PDB; 3PIP; X-ray; 3.45 A; R=1-115.
DR   PDB; 4IO9; X-ray; 3.20 A; R=1-115.
DR   PDB; 4IOA; X-ray; 3.20 A; R=1-115.
DR   PDB; 4IOC; X-ray; 3.60 A; R=1-115.
DR   PDB; 4U67; X-ray; 3.65 A; R=2-115.
DR   PDB; 4V49; X-ray; 8.70 A; S=2-114.
DR   PDB; 4V4A; X-ray; 9.50 A; S=2-114.
DR   PDB; 4V4G; X-ray; 11.50 A; V=2-114.
DR   PDB; 4WFN; X-ray; 3.54 A; R=1-115.
DR   PDB; 5DM6; X-ray; 2.90 A; R=4-113.
DR   PDB; 5DM7; X-ray; 3.00 A; R=4-113.
DR   PDB; 5JVG; X-ray; 3.43 A; R=1-115.
DR   PDB; 5JVH; X-ray; 3.58 A; R=1-115.
DR   PDBsum; 1GS2; -.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
DR   PDBsum; 1SM1; -.
DR   PDBsum; 1XBP; -.
DR   PDBsum; 2D3O; -.
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; Q9RXJ1; -.
DR   STRING; 243230.DR_0322; -.
DR   PRIDE; Q9RXJ1; -.
DR   EnsemblBacteria; AAF09903; AAF09903; DR_0322.
DR   GeneID; 1798682; -.
DR   KEGG; dra:DR_0322; -.
DR   PATRIC; fig|243230.17.peg.488; -.
DR   eggNOG; ENOG4105KAR; Bacteria.
DR   eggNOG; COG0198; LUCA.
DR   HOGENOM; HOG000039891; -.
DR   InParanoid; Q9RXJ1; -.
DR   KO; K02895; -.
DR   OMA; HVKPTQE; -.
DR   OrthoDB; 2040741at2; -.
DR   EvolutionaryTrace; Q9RXJ1; -.
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; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041988; KOW_RPL26/RPL24.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR003256; Ribosomal_L24.
DR   InterPro; IPR005825; Ribosomal_L24/26_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR12903; PTHR12903; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01079; rplX_bact; 1.
DR   PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9RXJ1.
DR   SWISS-2DPAGE; Q9RXJ1.
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..115
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_0000130653"
FT   HELIX           6..10
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          21..23
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   TURN            28..31
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          33..40
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   TURN            41..44
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          45..48
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          53..56
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          62..64
FT                   /evidence="ECO:0000244|PDB:2ZJR"
FT   STRAND          69..72
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   HELIX           78..80
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   TURN            86..88
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          95..99
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   TURN            100..102
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          103..107
FT                   /evidence="ECO:0000244|PDB:5DM6"
FT   STRAND          108..110
FT                   /evidence="ECO:0000244|PDB:2ZJR"
SQ   SEQUENCE   115 AA;  12358 MW;  FE0A0ABC51477BE1 CRC64;
     MPRPSAGSHH NDKLHFKKGD TVIVLSGKHK GQTGKVLLAL PRDQKVVVEG VNVITKNVKP
     SMTNPQGGQE QRELALHASK VALVDPETGK ATRVRKQIVD GKKVRVAVAS GKTID
//

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