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   27-MAR-2024, entry version 148.
DE   RecName: Full=Large ribosomal subunit protein eL39 {ECO:0000305};
DE   AltName: 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   PaxDb; 272569-rrnAC3112; -.
DR   EnsemblBacteria; AAV47823; AAV47823; rrnAC3112.
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   EvolutionaryTrace; P22452; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L39e; 1.
DR   HAMAP; MF_00629; Ribosomal_eL39; 1.
DR   InterPro; IPR000077; Ribosomal_eL39.
DR   InterPro; IPR020083; Ribosomal_eL39_CS.
DR   InterPro; IPR023626; Ribosomal_eL39_dom_sf.
DR   PANTHER; PTHR19970:SF0; 60S RIBOSOMAL PROTEIN L39; 1.
DR   PANTHER; PTHR19970; RIBOSOMAL PROTEIN L39E; 1.
DR   Pfam; PF00832; Ribosomal_L39; 1.
DR   SUPFAM; SSF48662; Ribosomal protein L39e; 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="Large ribosomal subunit protein eL39"
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
//