RL39_HALMA
ID RL39_HALMA Reviewed; 50 AA.
AC P22452; Q5UY30;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=50S ribosomal protein L39e;
DE AltName: Full=Hl39e;
DE AltName: Full=Hl46e;
GN Name=rpl39e; OrderedLocusNames=rrnAC3112;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-50.
RX PubMed=2207169; DOI=10.1016/0167-4781(90)90141-n;
RA Bergmann U., Arndt E.;
RT "Evidence for an additional archaebacterial gene cluster in Halobacterium
RT marismortui encoding ribosomal proteins HL46e and HL30.";
RL Biochim. Biophys. Acta 1050:56-60(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937989; DOI=10.1126/science.289.5481.905;
RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.;
RT "The complete atomic structure of the large ribosomal subunit at 2.4 A
RT resolution.";
RL Science 289:905-920(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937990; DOI=10.1126/science.289.5481.920;
RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.;
RT "The structural basis of ribosome activity in peptide bond synthesis.";
RL Science 289:920-930(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11828326; DOI=10.1038/nsb758;
RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K.,
RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.;
RT "A pre-translocational intermediate in protein synthesis observed in
RT crystals of enzymatically active 50S subunits.";
RL Nat. Struct. Biol. 9:225-230(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11483524; DOI=10.1093/emboj/20.15.4214;
RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "The kink-turn: a new RNA secondary structure motif.";
RL EMBO J. 20:4214-4221(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FOUR MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT "The structures of four macrolide antibiotics bound to the large ribosomal
RT subunit.";
RL Mol. Cell 10:117-128(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12185246; DOI=10.1073/pnas.172404099;
RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structural insights into peptide bond formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5;
RA Hansen J.L., Moore P.B., Steitz T.A.;
RT "Structures of five antibiotics bound at the peptidyl transferase center of
RT the large ribosomal subunit.";
RL J. Mol. Biol. 330:1061-1075(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT
RP E SITE SUBSTRATES.
RX PubMed=14561884; DOI=10.1261/rna.5120503;
RA Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structures of deacylated tRNA mimics bound to the E site of the large
RT ribosomal subunit.";
RL RNA 9:1345-1352(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX PubMed=23695244; DOI=10.1107/s0907444913004745;
RA Gabdulkhakov A., Nikonov S., Garber M.;
RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL Acta Crystallogr. D 69:997-1004(2013).
CC -!- FUNCTION: Binds to the 23S rRNA. Forms part of the polypeptide exit
CC tunnel.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC protein L23. {ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.
CC {ECO:0000305}.
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DR EMBL; X55007; CAA38750.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV47823.1; -; Genomic_DNA.
DR PIR; S13066; R6HS39.
DR RefSeq; WP_004518346.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; Y=2-50.
DR PDB; 1JJ2; X-ray; 2.40 A; 1=2-49.
DR PDB; 1K73; X-ray; 3.01 A; 3=2-49.
DR PDB; 1K8A; X-ray; 3.00 A; 3=2-49.
DR PDB; 1K9M; X-ray; 3.00 A; 3=2-49.
DR PDB; 1KC8; X-ray; 3.01 A; 3=2-49.
DR PDB; 1KD1; X-ray; 3.00 A; 3=2-49.
DR PDB; 1KQS; X-ray; 3.10 A; 1=2-49.
DR PDB; 1M1K; X-ray; 3.20 A; 3=2-49.
DR PDB; 1M90; X-ray; 2.80 A; 3=2-49.
DR PDB; 1N8R; X-ray; 3.00 A; 3=2-49.
DR PDB; 1NJI; X-ray; 3.00 A; 3=2-49.
DR PDB; 1Q7Y; X-ray; 3.20 A; 3=2-49.
DR PDB; 1Q81; X-ray; 2.95 A; 3=2-49.
DR PDB; 1Q82; X-ray; 2.98 A; 3=2-49.
DR PDB; 1Q86; X-ray; 3.00 A; 3=2-49.
DR PDB; 1QVF; X-ray; 3.10 A; 1=2-49.
DR PDB; 1QVG; X-ray; 2.90 A; 1=2-49.
DR PDB; 1S72; X-ray; 2.40 A; 2=1-50.
DR PDB; 1VQ4; X-ray; 2.70 A; 2=1-50.
DR PDB; 1VQ5; X-ray; 2.60 A; 2=1-50.
DR PDB; 1VQ6; X-ray; 2.70 A; 2=1-50.
DR PDB; 1VQ7; X-ray; 2.50 A; 2=1-50.
DR PDB; 1VQ8; X-ray; 2.20 A; 2=1-50.
DR PDB; 1VQ9; X-ray; 2.40 A; 2=1-50.
DR PDB; 1VQK; X-ray; 2.30 A; 2=1-50.
DR PDB; 1VQL; X-ray; 2.30 A; 2=1-50.
DR PDB; 1VQM; X-ray; 2.30 A; 2=1-50.
DR PDB; 1VQN; X-ray; 2.40 A; 2=1-50.
DR PDB; 1VQO; X-ray; 2.20 A; 2=1-50.
DR PDB; 1VQP; X-ray; 2.25 A; 2=1-50.
DR PDB; 1W2B; X-ray; 3.50 A; 1=2-49.
DR PDB; 1YHQ; X-ray; 2.40 A; 2=1-50.
DR PDB; 1YI2; X-ray; 2.65 A; 2=1-50.
DR PDB; 1YIJ; X-ray; 2.60 A; 2=1-50.
DR PDB; 1YIT; X-ray; 2.80 A; 2=1-50.
DR PDB; 1YJ9; X-ray; 2.90 A; 2=1-50.
DR PDB; 1YJN; X-ray; 3.00 A; 2=1-50.
DR PDB; 1YJW; X-ray; 2.90 A; 2=1-50.
DR PDB; 2OTJ; X-ray; 2.90 A; 2=1-50.
DR PDB; 2OTL; X-ray; 2.70 A; 2=1-50.
DR PDB; 2QA4; X-ray; 3.00 A; 2=1-50.
DR PDB; 2QEX; X-ray; 2.90 A; 2=1-50.
DR PDB; 3CC2; X-ray; 2.40 A; 2=1-50.
DR PDB; 3CC4; X-ray; 2.70 A; 2=1-50.
DR PDB; 3CC7; X-ray; 2.70 A; 2=1-50.
DR PDB; 3CCE; X-ray; 2.75 A; 2=1-50.
DR PDB; 3CCJ; X-ray; 2.70 A; 2=1-50.
DR PDB; 3CCL; X-ray; 2.90 A; 2=1-50.
DR PDB; 3CCM; X-ray; 2.55 A; 2=1-50.
DR PDB; 3CCQ; X-ray; 2.90 A; 2=1-50.
DR PDB; 3CCR; X-ray; 3.00 A; 2=1-50.
DR PDB; 3CCS; X-ray; 2.95 A; 2=1-50.
DR PDB; 3CCU; X-ray; 2.80 A; 2=1-50.
DR PDB; 3CCV; X-ray; 2.90 A; 2=1-50.
DR PDB; 3CD6; X-ray; 2.75 A; 2=1-50.
DR PDB; 3CMA; X-ray; 2.80 A; 2=1-50.
DR PDB; 3CME; X-ray; 2.95 A; 2=1-50.
DR PDB; 3CPW; X-ray; 2.70 A; 1=1-50.
DR PDB; 3CXC; X-ray; 3.00 A; 1=2-50.
DR PDB; 3G4S; X-ray; 3.20 A; 2=1-50.
DR PDB; 3G6E; X-ray; 2.70 A; 2=1-50.
DR PDB; 3G71; X-ray; 2.85 A; 2=1-50.
DR PDB; 3I55; X-ray; 3.11 A; 2=1-50.
DR PDB; 3I56; X-ray; 2.90 A; 2=1-50.
DR PDB; 3OW2; X-ray; 2.70 A; 1=2-50.
DR PDB; 4ADX; EM; 6.60 A; 2=1-50.
DR PDB; 4V9F; X-ray; 2.40 A; 2=1-50.
DR PDBsum; 1FFK; -.
DR PDBsum; 1JJ2; -.
DR PDBsum; 1K73; -.
DR PDBsum; 1K8A; -.
DR PDBsum; 1K9M; -.
DR PDBsum; 1KC8; -.
DR PDBsum; 1KD1; -.
DR PDBsum; 1KQS; -.
DR PDBsum; 1M1K; -.
DR PDBsum; 1M90; -.
DR PDBsum; 1N8R; -.
DR PDBsum; 1NJI; -.
DR PDBsum; 1Q7Y; -.
DR PDBsum; 1Q81; -.
DR PDBsum; 1Q82; -.
DR PDBsum; 1Q86; -.
DR PDBsum; 1QVF; -.
DR PDBsum; 1QVG; -.
DR PDBsum; 1S72; -.
DR PDBsum; 1VQ4; -.
DR PDBsum; 1VQ5; -.
DR PDBsum; 1VQ6; -.
DR PDBsum; 1VQ7; -.
DR PDBsum; 1VQ8; -.
DR PDBsum; 1VQ9; -.
DR PDBsum; 1VQK; -.
DR PDBsum; 1VQL; -.
DR PDBsum; 1VQM; -.
DR PDBsum; 1VQN; -.
DR PDBsum; 1VQO; -.
DR PDBsum; 1VQP; -.
DR PDBsum; 1W2B; -.
DR PDBsum; 1YHQ; -.
DR PDBsum; 1YI2; -.
DR PDBsum; 1YIJ; -.
DR PDBsum; 1YIT; -.
DR PDBsum; 1YJ9; -.
DR PDBsum; 1YJN; -.
DR PDBsum; 1YJW; -.
DR PDBsum; 2OTJ; -.
DR PDBsum; 2OTL; -.
DR PDBsum; 2QA4; -.
DR PDBsum; 2QEX; -.
DR PDBsum; 3CC2; -.
DR PDBsum; 3CC4; -.
DR PDBsum; 3CC7; -.
DR PDBsum; 3CCE; -.
DR PDBsum; 3CCJ; -.
DR PDBsum; 3CCL; -.
DR PDBsum; 3CCM; -.
DR PDBsum; 3CCQ; -.
DR PDBsum; 3CCR; -.
DR PDBsum; 3CCS; -.
DR PDBsum; 3CCU; -.
DR PDBsum; 3CCV; -.
DR PDBsum; 3CD6; -.
DR PDBsum; 3CMA; -.
DR PDBsum; 3CME; -.
DR PDBsum; 3CPW; -.
DR PDBsum; 3CXC; -.
DR PDBsum; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 3OW2; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P22452; -.
DR SMR; P22452; -.
DR IntAct; P22452; 2.
DR STRING; 272569.rrnAC3112; -.
DR EnsemblBacteria; AAV47823; AAV47823; rrnAC3112.
DR GeneID; 40153923; -.
DR GeneID; 64823662; -.
DR KEGG; hma:rrnAC3112; -.
DR PATRIC; fig|272569.17.peg.3654; -.
DR eggNOG; arCOG04177; Archaea.
DR HOGENOM; CLU_181948_4_0_2; -.
DR OMA; PAWVIMK; -.
DR EvolutionaryTrace; P22452; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 Gene3D; 1.10.1620.10; -; 1.
DR HAMAP; MF_00629; Ribosomal_L39e; 1.
DR InterPro; IPR000077; Ribosomal_L39.
DR InterPro; IPR020083; Ribosomal_L39_CS.
DR InterPro; IPR023626; Ribosomal_L39e_dom_sf.
DR Pfam; PF00832; Ribosomal_L39; 1.
DR SUPFAM; SSF48662; SSF48662; 1.
DR PROSITE; PS00051; RIBOSOMAL_L39E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2207169"
FT CHAIN 2..50
FT /note="50S ribosomal protein L39e"
FT /id="PRO_0000127047"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1YJ9"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 50 AA; 6115 MW; 4999D410AB7B331A CRC64;
MGKKSKATKK RLAKLDNQNS RVPAWVMLKT DREVQRNHKR RHWRRNDTDE
