ID RL18_HALMA Reviewed; 187 AA. AC P14123; Q5V1U1; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 161. DE RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L18; DE AltName: Full=Hl12; DE AltName: Full=Hmal18; GN Name=rpl18; OrderedLocusNames=rrnAC1593; 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=1832208; DOI=10.1007/bf00282450; RA Scholzen T., Arndt E.; RT "Organization and nucleotide sequence of ten ribosomal protein genes from RT the region equivalent to the spectinomycin operon in the archaebacterium RT Halobacterium marismortui."; RL Mol. Gen. Genet. 228:70-80(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 2-25. 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 [4] RP CROSS-LINKING TO L21E. 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 [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=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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 one of 5 proteins that mediate the attachment of the CC 5S rRNA onto the large ribosomal subunit, where it forms part of the CC central protuberance and stabilizes the orientation of adjacent RNA CC domains. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with proteins L5 CC and L21e, and attaches the 5S rRNA to the 23S rRNA. Has been cross- CC linked to L21e. {ECO:0000269|PubMed:12150912, CC ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 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; X58395; CAA41290.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46511.1; -; Genomic_DNA. DR PIR; S16541; R5HS18. DR RefSeq; WP_011223738.1; NZ_CP039138.1. DR PDB; 1FFK; X-ray; 2.40 A; K=2-186. DR PDB; 1JJ2; X-ray; 2.40 A; M=2-187. DR PDB; 1K73; X-ray; 3.01 A; O=2-187. DR PDB; 1K8A; X-ray; 3.00 A; O=2-187. DR PDB; 1K9M; X-ray; 3.00 A; O=2-187. DR PDB; 1KC8; X-ray; 3.01 A; O=2-187. DR PDB; 1KD1; X-ray; 3.00 A; O=2-187. DR PDB; 1KQS; X-ray; 3.10 A; M=2-187. DR PDB; 1M1K; X-ray; 3.20 A; O=2-187. DR PDB; 1M90; X-ray; 2.80 A; O=2-187. DR PDB; 1ML5; EM; 14.00 A; q=2-187. DR PDB; 1N8R; X-ray; 3.00 A; O=2-187. DR PDB; 1NJI; X-ray; 3.00 A; O=2-187. DR PDB; 1Q7Y; X-ray; 3.20 A; O=2-187. DR PDB; 1Q81; X-ray; 2.95 A; O=2-187. DR PDB; 1Q82; X-ray; 2.98 A; O=2-187. DR PDB; 1Q86; X-ray; 3.00 A; O=2-187. DR PDB; 1QVF; X-ray; 3.10 A; M=2-187. DR PDB; 1QVG; X-ray; 2.90 A; M=2-187. DR PDB; 1S72; X-ray; 2.40 A; N=1-187. DR PDB; 1VQ4; X-ray; 2.70 A; N=1-187. DR PDB; 1VQ5; X-ray; 2.60 A; N=1-187. DR PDB; 1VQ6; X-ray; 2.70 A; N=1-187. DR PDB; 1VQ7; X-ray; 2.50 A; N=1-187. DR PDB; 1VQ8; X-ray; 2.20 A; N=1-187. DR PDB; 1VQ9; X-ray; 2.40 A; N=1-187. DR PDB; 1VQK; X-ray; 2.30 A; N=1-187. DR PDB; 1VQL; X-ray; 2.30 A; N=1-187. DR PDB; 1VQM; X-ray; 2.30 A; N=1-187. DR PDB; 1VQN; X-ray; 2.40 A; N=1-187. DR PDB; 1VQO; X-ray; 2.20 A; N=1-187. DR PDB; 1VQP; X-ray; 2.25 A; N=1-187. DR PDB; 1W2B; X-ray; 3.50 A; M=2-187. DR PDB; 1YHQ; X-ray; 2.40 A; N=1-187. DR PDB; 1YI2; X-ray; 2.65 A; N=1-187. DR PDB; 1YIJ; X-ray; 2.60 A; N=1-187. DR PDB; 1YIT; X-ray; 2.80 A; N=1-187. DR PDB; 1YJ9; X-ray; 2.90 A; N=1-187. DR PDB; 1YJN; X-ray; 3.00 A; N=1-187. DR PDB; 1YJW; X-ray; 2.90 A; N=1-187. DR PDB; 2OTJ; X-ray; 2.90 A; N=1-187. DR PDB; 2OTL; X-ray; 2.70 A; N=1-187. DR PDB; 2QA4; X-ray; 3.00 A; N=1-187. DR PDB; 2QEX; X-ray; 2.90 A; N=1-187. DR PDB; 3CC2; X-ray; 2.40 A; N=1-187. DR PDB; 3CC4; X-ray; 2.70 A; N=1-187. DR PDB; 3CC7; X-ray; 2.70 A; N=1-187. DR PDB; 3CCE; X-ray; 2.75 A; N=1-187. DR PDB; 3CCJ; X-ray; 2.70 A; N=1-187. DR PDB; 3CCL; X-ray; 2.90 A; N=1-187. DR PDB; 3CCM; X-ray; 2.55 A; N=1-187. DR PDB; 3CCQ; X-ray; 2.90 A; N=1-187. DR PDB; 3CCR; X-ray; 3.00 A; N=1-187. DR PDB; 3CCS; X-ray; 2.95 A; N=1-187. DR PDB; 3CCU; X-ray; 2.80 A; N=1-187. DR PDB; 3CCV; X-ray; 2.90 A; N=1-187. DR PDB; 3CD6; X-ray; 2.75 A; N=1-187. DR PDB; 3CMA; X-ray; 2.80 A; N=1-187. DR PDB; 3CME; X-ray; 2.95 A; N=1-187. DR PDB; 3CPW; X-ray; 2.70 A; M=1-187. DR PDB; 3CXC; X-ray; 3.00 A; M=2-187. DR PDB; 3G4S; X-ray; 3.20 A; N=2-187. DR PDB; 3G6E; X-ray; 2.70 A; N=2-187. DR PDB; 3G71; X-ray; 2.85 A; N=2-187. DR PDB; 3I55; X-ray; 3.11 A; N=1-187. DR PDB; 3I56; X-ray; 2.90 A; N=1-187. DR PDB; 3OW2; X-ray; 2.70 A; M=2-187. DR PDB; 4ADX; EM; 6.60 A; N=1-187. DR PDB; 4V42; X-ray; 5.50 A; BQ=2-187. DR PDB; 4V4R; X-ray; 5.90 A; S=2-187. DR PDB; 4V4S; X-ray; 6.76 A; S=2-187. DR PDB; 4V4T; X-ray; 6.46 A; S=2-187. DR PDB; 4V9F; X-ray; 2.40 A; N=1-187. 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; 3CXC; -. DR PDBsum; 3G4S; -. DR PDBsum; 3G6E; -. DR PDBsum; 3G71; -. DR PDBsum; 3I55; -. DR PDBsum; 3I56; -. DR PDBsum; 3OW2; -. DR PDBsum; 4ADX; -. DR PDBsum; 4V42; -. DR PDBsum; 4V4R; -. DR PDBsum; 4V4S; -. DR PDBsum; 4V4T; -. DR PDBsum; 4V9F; -. DR AlphaFoldDB; P14123; -. DR SMR; P14123; -. DR IntAct; P14123; 3. DR STRING; 272569.rrnAC1593; -. DR PaxDb; 272569-rrnAC1593; -. DR EnsemblBacteria; AAV46511; AAV46511; rrnAC1593. DR GeneID; 64821834; -. DR KEGG; hma:rrnAC1593; -. DR PATRIC; fig|272569.17.peg.2282; -. DR eggNOG; arCOG04088; Archaea. DR HOGENOM; CLU_056222_2_0_2; -. DR EvolutionaryTrace; P14123; -. 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:0008097; F:5S rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd00432; Ribosomal_L18_L5e; 1. DR Gene3D; 3.30.420.100; -; 1. DR HAMAP; MF_01337_A; Ribosomal_uL18_A; 1. DR InterPro; IPR005485; Rbsml_uL18_euk/arc. DR PANTHER; PTHR23410:SF12; 60S RIBOSOMAL PROTEIN L5; 1. DR PANTHER; PTHR23410; RIBOSOMAL PROTEIN L5-RELATED; 1. DR Pfam; PF17144; Ribosomal_L5e; 2. DR PRINTS; PR00058; RIBOSOMALL5. DR SUPFAM; SSF53137; Translational machinery components; 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 CHAIN 2..187 FT /note="Large ribosomal subunit protein uL18" FT /id="PRO_0000131400" FT CONFLICT 18 FT /note="R -> A (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:3OW2" FT HELIX 12..15 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 21..28 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 44..50 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:3CC2" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 65..70 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 79..95 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 115..125 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 140..144 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 146..153 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:1VQ8" FT HELIX 170..181 FT /evidence="ECO:0007829|PDB:1VQ8" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:1VQ8" SQ SEQUENCE 187 AA; 20614 MW; 60E9AF3CB64E7CA5 CRC64; MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT LGPNGDDTLA SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE AVLDIGLNSP TPGSKVFAIQ EGAIDAGLDI PHNDDVLADW QRTRGAHIAE YDEQLEEPLY SGDFDAADLP EHFDELRETL LDGDIEL //