RL18_HALMA
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 25-MAY-2022, entry version 154.
DE RecName: 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}.
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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 EnsemblBacteria; AAV46511; AAV46511; rrnAC1593.
DR GeneID; 40152558; -.
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 OMA; MAHGPRY; -.
DR EvolutionaryTrace; P14123; -.
DR Proteomes; UP000001169; Chromosome I.
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 HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF17144; Ribosomal_L5e; 2.
DR PRINTS; PR00058; RIBOSOMALL5.
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="50S ribosomal protein L18"
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
