RL10E_HALMA
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 25-MAY-2022, entry version 117.
DE RecName: Full=50S ribosomal protein L10e {ECO:0000255|HAMAP-Rule:MF_00448};
GN Name=rpl10e {ECO:0000255|HAMAP-Rule:MF_00448}; 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 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 OMA; HHVIREN; -.
DR EvolutionaryTrace; P60617; -.
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: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; -; 1.
DR HAMAP; MF_00448; Ribosomal_L10e; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR022981; Ribosomal_L10e_arc.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 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="50S ribosomal protein L10e"
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
