RL14_DEIRA
ID RL14_DEIRA Reviewed; 134 AA.
AC Q9RXJ2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; OrderedLocusNames=DR_0321;
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: Forms part of two intersubunit bridges in the 70S ribosome
CC (By similarity). Binds to 23S rRNA. {ECO:0000250}.
CC -!- SUBUNIT: In the 70S ribosome, L14 and L19 interact and together make
CC contacts with the 16S rRNA in bridges B5 and B8 (By similarity). Part
CC of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19.
CC {ECO:0000250, 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 uL14 family.
CC {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR EMBL; AE000513; AAF09902.1; -; Genomic_DNA.
DR PIR; A75535; A75535.
DR RefSeq; NP_294044.1; NC_001263.1.
DR RefSeq; WP_010886966.1; NZ_CP015081.1.
DR PDB; 1NKW; X-ray; 3.10 A; I=1-134.
DR PDB; 1NWX; X-ray; 3.50 A; I=1-134.
DR PDB; 1NWY; X-ray; 3.30 A; I=1-134.
DR PDB; 1SM1; X-ray; 3.42 A; I=1-134.
DR PDB; 1XBP; X-ray; 3.50 A; I=1-134.
DR PDB; 2ZJP; X-ray; 3.70 A; H=1-134.
DR PDB; 2ZJQ; X-ray; 3.30 A; H=1-134.
DR PDB; 2ZJR; X-ray; 2.91 A; H=1-134.
DR PDB; 3CF5; X-ray; 3.30 A; H=1-134.
DR PDB; 3DLL; X-ray; 3.50 A; H=1-134.
DR PDB; 3PIO; X-ray; 3.25 A; H=1-134.
DR PDB; 3PIP; X-ray; 3.45 A; H=1-134.
DR PDB; 4IO9; X-ray; 3.20 A; H=1-134.
DR PDB; 4IOA; X-ray; 3.20 A; H=1-134.
DR PDB; 4IOC; X-ray; 3.60 A; H=1-134.
DR PDB; 4U67; X-ray; 3.65 A; H=1-134.
DR PDB; 4V49; X-ray; 8.70 A; I=2-133.
DR PDB; 4V4A; X-ray; 9.50 A; I=2-133.
DR PDB; 4V4G; X-ray; 11.50 A; L=2-133.
DR PDB; 4WFN; X-ray; 3.54 A; H=1-134.
DR PDB; 5DM6; X-ray; 2.90 A; H=1-134.
DR PDB; 5DM7; X-ray; 3.00 A; H=1-134.
DR PDB; 5JVG; X-ray; 3.43 A; H=1-134.
DR PDB; 5JVH; X-ray; 3.58 A; H=1-134.
DR PDB; 7A0R; X-ray; 3.30 A; H=1-134.
DR PDB; 7A0S; X-ray; 3.22 A; H=1-134.
DR PDB; 7A18; X-ray; 3.40 A; H=1-134.
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; Q9RXJ2; -.
DR SMR; Q9RXJ2; -.
DR IntAct; Q9RXJ2; 1.
DR STRING; 243230.DR_0321; -.
DR PRIDE; Q9RXJ2; -.
DR EnsemblBacteria; AAF09902; AAF09902; DR_0321.
DR KEGG; dra:DR_0321; -.
DR PATRIC; fig|243230.17.peg.487; -.
DR eggNOG; COG0093; Bacteria.
DR HOGENOM; CLU_095071_2_1_0; -.
DR InParanoid; Q9RXJ2; -.
DR OMA; AKEVLCI; -.
DR OrthoDB; 1799923at2; -.
DR EvolutionaryTrace; Q9RXJ2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR TIGRFAMs; TIGR01067; rplN_bact; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 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..134
FT /note="50S ribosomal protein L14"
FT /id="PRO_0000128539"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3PIP"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7A0S"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4IO9"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4IO9"
SQ SEQUENCE 134 AA; 14232 MW; A28B8DF0FD84100F CRC64;
MIMPQSRLDV ADNSGAREIM CIRVLNSGIG GKGLTTGGGG NKRYAHVGDI IVASVKDAAP
RGAVKAGDVV KAVVVRTSHA IKRADGSTIR FDRNAAVIIN NQGEPRGTRV FGPVARELRD
RRFMKIVSLA PEVL
