RL18E_HALMA
ID RL18E_HALMA Reviewed; 116 AA.
AC P12733; Q5V5Q8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=50S ribosomal protein L18e;
DE AltName: Full=Hl29;
DE AltName: Full=L19;
GN Name=rpl18e; OrderedLocusNames=rrnAC0064;
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].
RX PubMed=1840597; DOI=10.1016/s0021-9258(18)54267-8;
RA Kroemer W.J., Arndt E.;
RT "Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed
RT with genes encoding a tRNA(Leu), the enolase, and a putative membrane
RT protein in the archaebacterium Haloarcula (Halobacterium) marismortui.";
RL J. Biol. Chem. 266:24573-24579(1991).
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 PROTEIN SEQUENCE OF 2-116.
RX PubMed=3350019; DOI=10.1111/j.1432-1033.1988.tb13945.x;
RA Hatakeyama T., Kimura M.;
RT "Complete amino acid sequences of the ribosomal proteins L25, L29 and L31
RT from the archaebacterium Halobacterium marismortui.";
RL Eur. J. Biochem. 172:703-711(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RX PubMed=1376318; DOI=10.1016/s0021-9258(19)49814-1;
RA Scholzen T., Arndt E.;
RT "The alpha-operon equivalent genome region in the extreme halophilic
RT archaebacterium Haloarcula (Halobacterium) marismortui.";
RL J. Biol. Chem. 267:12123-12130(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3196689; DOI=10.1021/bi00418a032;
RA Walsh M.J., McDougall J., Wittmann-Liebold B.;
RT "Extended N-terminal sequencing of proteins of archaebacterial ribosomes
RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT difluoride) membrane.";
RL Biochemistry 27:6867-6876(1988).
RN [6]
RP PROTEIN SEQUENCE OF 4-27; 37-39 AND 65-82, AND CROSS-LINKING TO L4.
RX PubMed=8345527; DOI=10.1006/jmbi.1993.1419;
RA Bergmann U., Wittmann-Liebold B.;
RT "Localization of proteins HL29 and HL31 from Haloarcula marismortui within
RT the 50 S ribosomal subunit by chemical crosslinking.";
RL J. Mol. Biol. 232:693-700(1993).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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: Stabilizes the tertiary rRNA structure within the 23S rRNA
CC domain (domain II) to which it binds.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC proteins L4 and L15. Has been cross-linked to L4.
CC {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M76567; AAA73096.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV45144.1; -; Genomic_DNA.
DR EMBL; M87833; AAA73213.1; -; Genomic_DNA.
DR PIR; A41715; R5HSH9.
DR RefSeq; WP_004516800.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; L=2-116.
DR PDB; 1JJ2; X-ray; 2.40 A; N=2-116.
DR PDB; 1K73; X-ray; 3.01 A; P=2-116.
DR PDB; 1K8A; X-ray; 3.00 A; P=2-116.
DR PDB; 1K9M; X-ray; 3.00 A; P=2-116.
DR PDB; 1KC8; X-ray; 3.01 A; P=2-116.
DR PDB; 1KD1; X-ray; 3.00 A; P=2-116.
DR PDB; 1KQS; X-ray; 3.10 A; N=2-116.
DR PDB; 1M1K; X-ray; 3.20 A; P=2-116.
DR PDB; 1M90; X-ray; 2.80 A; P=2-116.
DR PDB; 1N8R; X-ray; 3.00 A; P=2-116.
DR PDB; 1NJI; X-ray; 3.00 A; P=2-116.
DR PDB; 1Q7Y; X-ray; 3.20 A; P=2-116.
DR PDB; 1Q81; X-ray; 2.95 A; P=2-116.
DR PDB; 1Q82; X-ray; 2.98 A; P=2-116.
DR PDB; 1Q86; X-ray; 3.00 A; P=2-116.
DR PDB; 1QVF; X-ray; 3.10 A; N=2-116.
DR PDB; 1QVG; X-ray; 2.90 A; N=2-116.
DR PDB; 1S72; X-ray; 2.40 A; O=1-116.
DR PDB; 1VQ4; X-ray; 2.70 A; O=1-116.
DR PDB; 1VQ5; X-ray; 2.60 A; O=1-116.
DR PDB; 1VQ6; X-ray; 2.70 A; O=1-116.
DR PDB; 1VQ7; X-ray; 2.50 A; O=1-116.
DR PDB; 1VQ8; X-ray; 2.20 A; O=1-116.
DR PDB; 1VQ9; X-ray; 2.40 A; O=1-116.
DR PDB; 1VQK; X-ray; 2.30 A; O=1-116.
DR PDB; 1VQL; X-ray; 2.30 A; O=1-116.
DR PDB; 1VQM; X-ray; 2.30 A; O=1-116.
DR PDB; 1VQN; X-ray; 2.40 A; O=1-116.
DR PDB; 1VQO; X-ray; 2.20 A; O=1-116.
DR PDB; 1VQP; X-ray; 2.25 A; O=1-116.
DR PDB; 1W2B; X-ray; 3.50 A; N=2-116.
DR PDB; 1YHQ; X-ray; 2.40 A; O=1-116.
DR PDB; 1YI2; X-ray; 2.65 A; O=1-116.
DR PDB; 1YIJ; X-ray; 2.60 A; O=1-116.
DR PDB; 1YIT; X-ray; 2.80 A; O=1-116.
DR PDB; 1YJ9; X-ray; 2.90 A; O=1-116.
DR PDB; 1YJN; X-ray; 3.00 A; O=1-116.
DR PDB; 1YJW; X-ray; 2.90 A; O=1-116.
DR PDB; 2OTJ; X-ray; 2.90 A; O=1-116.
DR PDB; 2OTL; X-ray; 2.70 A; O=1-116.
DR PDB; 2QA4; X-ray; 3.00 A; O=1-116.
DR PDB; 2QEX; X-ray; 2.90 A; O=1-116.
DR PDB; 3CC2; X-ray; 2.40 A; O=1-116.
DR PDB; 3CC4; X-ray; 2.70 A; O=1-116.
DR PDB; 3CC7; X-ray; 2.70 A; O=1-116.
DR PDB; 3CCE; X-ray; 2.75 A; O=1-116.
DR PDB; 3CCJ; X-ray; 2.70 A; O=1-116.
DR PDB; 3CCL; X-ray; 2.90 A; O=1-116.
DR PDB; 3CCM; X-ray; 2.55 A; O=1-116.
DR PDB; 3CCQ; X-ray; 2.90 A; O=1-116.
DR PDB; 3CCR; X-ray; 3.00 A; O=1-116.
DR PDB; 3CCS; X-ray; 2.95 A; O=1-116.
DR PDB; 3CCU; X-ray; 2.80 A; O=1-116.
DR PDB; 3CCV; X-ray; 2.90 A; O=1-116.
DR PDB; 3CD6; X-ray; 2.75 A; O=1-116.
DR PDB; 3CMA; X-ray; 2.80 A; O=1-116.
DR PDB; 3CME; X-ray; 2.95 A; O=1-116.
DR PDB; 3CPW; X-ray; 2.70 A; N=1-116.
DR PDB; 3CXC; X-ray; 3.00 A; N=2-116.
DR PDB; 3G4S; X-ray; 3.20 A; O=2-116.
DR PDB; 3G6E; X-ray; 2.70 A; O=2-116.
DR PDB; 3G71; X-ray; 2.85 A; O=2-116.
DR PDB; 3I55; X-ray; 3.11 A; O=1-116.
DR PDB; 3I56; X-ray; 2.90 A; O=1-116.
DR PDB; 3OW2; X-ray; 2.70 A; N=2-116.
DR PDB; 4ADX; EM; 6.60 A; O=1-116.
DR PDB; 4V9F; X-ray; 2.40 A; O=1-116.
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; P12733; -.
DR SMR; P12733; -.
DR IntAct; P12733; 2.
DR STRING; 272569.rrnAC0064; -.
DR EnsemblBacteria; AAV45144; AAV45144; rrnAC0064.
DR GeneID; 40154379; -.
DR GeneID; 64823169; -.
DR KEGG; hma:rrnAC0064; -.
DR PATRIC; fig|272569.17.peg.872; -.
DR eggNOG; arCOG00780; Archaea.
DR HOGENOM; CLU_146465_0_0_2; -.
DR OMA; WRLERPR; -.
DR EvolutionaryTrace; P12733; -.
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 HAMAP; MF_00329; Ribosomal_L18e; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021132; Ribosomal_L18/L18-A/B/e_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR InterPro; IPR022947; Ribosomal_L18e_arc.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS01106; RIBOSOMAL_L18E; 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:3196689,
FT ECO:0000269|PubMed:3350019"
FT CHAIN 2..116
FT /note="50S ribosomal protein L18e"
FT /id="PRO_0000132787"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 116 AA; 12422 MW; BFACD702AE94474D CRC64;
MSKTNPRLSS LIADLKSAAR SSGGAVWGDV AERLEKPRRT HAEVNLGRIE RYAQEDETVV
VPGKVLGSGV LQKDVTVAAV DFSGTAETKI DQVGEAVSLE QAIENNPEGS HVRVIR
