ID   RL10E_HALMA             Reviewed;         177 AA.
AC   P60617; Q5UZX7;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Large ribosomal subunit protein uL16 {ECO:0000255|HAMAP-Rule:MF_00448};
DE   AltName: Full=50S ribosomal protein L10e {ECO:0000305};
GN   Name=rpl10e {ECO:0000255|HAMAP-Rule:MF_00448};
GN   OrderedLocusNames=rrnAC2357;
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 [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   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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: This is 1 of 5 proteins that mediate the attachment of the 5S
CC       rRNA onto the large ribosomal subunit, stabilizing the orientation of
CC       adjacent RNA domains. Modeling places the A and P site tRNAs in close
CC       proximity to this protein.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Weakly binds 5S rRNA.
CC       Probably binds the A and P site tRNAs. {ECO:0000269|PubMed:12150912,
CC       ECO:0000269|PubMed:12860128}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00448}.
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DR   EMBL; AY596297; AAV47175.1; -; Genomic_DNA.
DR   RefSeq; WP_007189393.1; NZ_CP039138.1.
DR   PDB; 1FFK; X-ray; 2.40 A; F=14-129.
DR   PDB; 1JJ2; X-ray; 2.40 A; H=14-130.
DR   PDB; 1K73; X-ray; 3.01 A; J=14-130.
DR   PDB; 1K8A; X-ray; 3.00 A; J=14-130.
DR   PDB; 1K9M; X-ray; 3.00 A; J=14-130.
DR   PDB; 1KC8; X-ray; 3.01 A; J=14-130.
DR   PDB; 1KD1; X-ray; 3.00 A; J=14-130.
DR   PDB; 1KQS; X-ray; 3.10 A; H=14-130.
DR   PDB; 1M1K; X-ray; 3.20 A; J=14-130.
DR   PDB; 1M90; X-ray; 2.80 A; J=14-130.
DR   PDB; 1ML5; EM; 14.00 A; p=18-129.
DR   PDB; 1N8R; X-ray; 3.00 A; J=14-130.
DR   PDB; 1NJI; X-ray; 3.00 A; J=14-130.
DR   PDB; 1Q7Y; X-ray; 3.20 A; J=14-130.
DR   PDB; 1Q81; X-ray; 2.95 A; J=14-130.
DR   PDB; 1Q82; X-ray; 2.98 A; J=14-130.
DR   PDB; 1Q86; X-ray; 3.00 A; J=14-130.
DR   PDB; 1QVF; X-ray; 3.10 A; H=14-130.
DR   PDB; 1QVG; X-ray; 2.90 A; H=14-130.
DR   PDB; 1S72; X-ray; 2.40 A; H=4-166.
DR   PDB; 1VQ4; X-ray; 2.70 A; H=4-166.
DR   PDB; 1VQ5; X-ray; 2.60 A; H=4-166.
DR   PDB; 1VQ6; X-ray; 2.70 A; H=4-166.
DR   PDB; 1VQ7; X-ray; 2.50 A; H=4-166.
DR   PDB; 1VQ8; X-ray; 2.20 A; H=4-166.
DR   PDB; 1VQ9; X-ray; 2.40 A; H=4-166.
DR   PDB; 1VQK; X-ray; 2.30 A; H=4-166.
DR   PDB; 1VQL; X-ray; 2.30 A; H=4-166.
DR   PDB; 1VQM; X-ray; 2.30 A; H=4-166.
DR   PDB; 1VQN; X-ray; 2.40 A; H=4-166.
DR   PDB; 1VQO; X-ray; 2.20 A; H=4-166.
DR   PDB; 1VQP; X-ray; 2.25 A; H=4-166.
DR   PDB; 1W2B; X-ray; 3.50 A; H=14-130.
DR   PDB; 1YHQ; X-ray; 2.40 A; H=1-177.
DR   PDB; 1YI2; X-ray; 2.65 A; H=1-177.
DR   PDB; 1YIJ; X-ray; 2.60 A; H=1-177.
DR   PDB; 1YIT; X-ray; 2.80 A; H=1-177.
DR   PDB; 1YJ9; X-ray; 2.90 A; H=1-177.
DR   PDB; 1YJN; X-ray; 3.00 A; H=1-177.
DR   PDB; 1YJW; X-ray; 2.90 A; H=1-177.
DR   PDB; 2OTJ; X-ray; 2.90 A; H=4-166.
DR   PDB; 2OTL; X-ray; 2.70 A; H=4-166.
DR   PDB; 2QA4; X-ray; 3.00 A; H=4-177.
DR   PDB; 2QEX; X-ray; 2.90 A; H=1-177.
DR   PDB; 3CC2; X-ray; 2.40 A; H=1-177.
DR   PDB; 3CC4; X-ray; 2.70 A; H=1-177.
DR   PDB; 3CC7; X-ray; 2.70 A; H=1-177.
DR   PDB; 3CCE; X-ray; 2.75 A; H=1-177.
DR   PDB; 3CCJ; X-ray; 2.70 A; H=1-177.
DR   PDB; 3CCL; X-ray; 2.90 A; H=1-177.
DR   PDB; 3CCM; X-ray; 2.55 A; H=1-177.
DR   PDB; 3CCQ; X-ray; 2.90 A; H=1-177.
DR   PDB; 3CCR; X-ray; 3.00 A; H=1-177.
DR   PDB; 3CCS; X-ray; 2.95 A; H=1-177.
DR   PDB; 3CCU; X-ray; 2.80 A; H=1-177.
DR   PDB; 3CCV; X-ray; 2.90 A; H=1-177.
DR   PDB; 3CD6; X-ray; 2.75 A; H=1-177.
DR   PDB; 3CMA; X-ray; 2.80 A; H=1-177.
DR   PDB; 3CME; X-ray; 2.95 A; H=1-177.
DR   PDB; 3CPW; X-ray; 2.70 A; H=1-177.
DR   PDB; 3G4S; X-ray; 3.20 A; H=1-177.
DR   PDB; 3G6E; X-ray; 2.70 A; H=1-177.
DR   PDB; 3G71; X-ray; 2.85 A; H=1-177.
DR   PDB; 3I55; X-ray; 3.11 A; H=1-166.
DR   PDB; 3I56; X-ray; 2.90 A; H=1-166.
DR   PDB; 4ADX; EM; 6.60 A; H=1-177.
DR   PDB; 4V9F; X-ray; 2.40 A; H=1-177.
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; 1ML5; -.
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; 3G4S; -.
DR   PDBsum; 3G6E; -.
DR   PDBsum; 3G71; -.
DR   PDBsum; 3I55; -.
DR   PDBsum; 3I56; -.
DR   PDBsum; 4ADX; -.
DR   PDBsum; 4V9F; -.
DR   AlphaFoldDB; P60617; -.
DR   SMR; P60617; -.
DR   IntAct; P60617; 27.
DR   STRING; 272569.rrnAC2357; -.
DR   PaxDb; 272569-rrnAC2357; -.
DR   EnsemblBacteria; AAV47175; AAV47175; rrnAC2357.
DR   GeneID; 40153255; -.
DR   KEGG; hma:rrnAC2357; -.
DR   PATRIC; fig|272569.17.peg.2976; -.
DR   eggNOG; arCOG04113; Archaea.
DR   HOGENOM; CLU_084051_0_2_2; -.
DR   EvolutionaryTrace; P60617; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01433; Ribosomal_L16_L10e; 1.
DR   Gene3D; 3.90.1170.10; Ribosomal protein L10e/L16; 1.
DR   HAMAP; MF_00448; Ribosomal_uL16_arch; 1.
DR   InterPro; IPR047873; Ribosomal_uL16.
DR   InterPro; IPR022981; Ribosomal_uL16_arc.
DR   InterPro; IPR018255; Ribosomal_uL16_CS_euk_arc.
DR   InterPro; IPR016180; Ribosomal_uL16_dom.
DR   InterPro; IPR001197; Ribosomal_uL16_euk_arch.
DR   InterPro; IPR036920; Ribosomal_uL16_sf.
DR   PANTHER; PTHR11726; 60S RIBOSOMAL PROTEIN L10; 1.
DR   PANTHER; PTHR11726:SF10; 60S RIBOSOMAL PROTEIN L10; 1.
DR   Pfam; PF00252; Ribosomal_L16; 1.
DR   PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR   SUPFAM; SSF54686; Ribosomal protein L16p/L10e; 1.
DR   PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..177
FT                   /note="Large ribosomal subunit protein uL16"
FT                   /id="PRO_0000147132"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:1VQO"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:1Q7Y"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1VQO"
FT   STRAND          47..56
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           62..80
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:1YJW"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1JJ2"
FT   STRAND          122..130
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:1VQ8"
SQ   SEQUENCE   177 AA;  19908 MW;  E7A72FE3683D2BDB CRC64;
     MSDKPASMYR DIDKPAYTRR EYITGIPGSK IAQHKMGRKQ KDADDYPVQI SLIVEETVQL
     RHGSLEASRL SANRHLIKEL GEEGDYKMTL RKFPHQVLRE NKQATGAGAD RVSDGMRAAF
     GKIVGTAARV QAGEQLFTAY CNVEDAEHVK EAFRRAYNKI TPSCRIKVER GEELLIA
//