ID RL23_HALMA Reviewed; 85 AA. AC P12732; Q5V1S6; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 31-JUL-2019, entry version 141. DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369}; DE AltName: Full=Hl25; DE AltName: Full=Hmal23; DE AltName: Full=L21; GN Name=rpl23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=rrnAC1609; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; OC Halobacteriales; Haloarculaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP PROTEIN SEQUENCE OF 2-85. 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 RT L31 from the archaebacterium Halobacterium marismortui."; RL Eur. J. Biochem. 172:703-711(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2406244; RA Arndt E., Kroemer W., Hatakeyama T.; RT "Organization and nucleotide sequence of a gene cluster coding for RT eight ribosomal proteins in the archaebacterium Halobacterium RT marismortui."; RL J. Biol. Chem. 265:3034-3039(1990). RN [3] 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., RA Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., RA Date S.V., Marcotte E., Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from RT the Dead Sea."; RL Genome Res. 14:2221-2234(2004). RN [4] RP PROTEIN SEQUENCE OF 2-23. 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 RT ribosomes blotted from two-dimensional gels onto glass fiber and RT poly(vinylidene difluoride) membrane."; RL Biochemistry 27:6867-6876(1988). 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 RT 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 RP WITH 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., RA Steitz T.A.; RT "The structures of four macrolide antibiotics bound to the large RT ribosomal 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 RP WITH 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 RT center of 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 RP DIFFERENT 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: Binds to a specific region on the 23S rRNA. Located at CC the polypeptide exit tunnel on the outside of the subunit. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein CC L29 and weakly with protein L39e. {ECO:0000255|HAMAP- CC Rule:MF_01369, ECO:0000269|PubMed:12150912, CC ECO:0000269|PubMed:12860128}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 CC family. {ECO:0000255|HAMAP-Rule:MF_01369}. 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; J05222; AAA86861.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46526.1; -; Genomic_DNA. DR PIR; E35063; R5HS23. DR RefSeq; WP_004591553.1; NC_006396.1. DR PDB; 1FFK; X-ray; 2.40 A; P=2-85. DR PDB; 1JJ2; X-ray; 2.40 A; R=2-85. DR PDB; 1K73; X-ray; 3.01 A; T=2-85. DR PDB; 1K8A; X-ray; 3.00 A; T=2-85. DR PDB; 1K9M; X-ray; 3.00 A; T=2-85. DR PDB; 1KC8; X-ray; 3.01 A; T=2-85. DR PDB; 1KD1; X-ray; 3.00 A; T=2-85. DR PDB; 1KQS; X-ray; 3.10 A; R=2-85. DR PDB; 1M1K; X-ray; 3.20 A; T=2-85. DR PDB; 1M90; X-ray; 2.80 A; T=2-85. DR PDB; 1N8R; X-ray; 3.00 A; T=2-85. DR PDB; 1NJI; X-ray; 3.00 A; T=2-85. DR PDB; 1Q7Y; X-ray; 3.20 A; T=2-85. DR PDB; 1Q81; X-ray; 2.95 A; T=2-85. DR PDB; 1Q82; X-ray; 2.98 A; T=2-85. DR PDB; 1Q86; X-ray; 3.00 A; T=2-85. DR PDB; 1QVF; X-ray; 3.10 A; R=2-85. DR PDB; 1QVG; X-ray; 2.90 A; R=2-85. DR PDB; 1S72; X-ray; 2.40 A; S=1-85. DR PDB; 1VQ4; X-ray; 2.70 A; S=1-85. DR PDB; 1VQ5; X-ray; 2.60 A; S=1-85. DR PDB; 1VQ6; X-ray; 2.70 A; S=1-85. DR PDB; 1VQ7; X-ray; 2.50 A; S=1-85. DR PDB; 1VQ8; X-ray; 2.20 A; S=1-85. DR PDB; 1VQ9; X-ray; 2.40 A; S=1-85. DR PDB; 1VQK; X-ray; 2.30 A; S=1-85. DR PDB; 1VQL; X-ray; 2.30 A; S=1-85. DR PDB; 1VQM; X-ray; 2.30 A; S=1-85. DR PDB; 1VQN; X-ray; 2.40 A; S=1-85. DR PDB; 1VQO; X-ray; 2.20 A; S=1-85. DR PDB; 1VQP; X-ray; 2.25 A; S=1-85. DR PDB; 1W2B; X-ray; 3.50 A; R=2-85. DR PDB; 1YHQ; X-ray; 2.40 A; S=1-85. DR PDB; 1YI2; X-ray; 2.65 A; S=1-85. DR PDB; 1YIJ; X-ray; 2.60 A; S=1-85. DR PDB; 1YIT; X-ray; 2.80 A; S=1-85. DR PDB; 1YJ9; X-ray; 2.90 A; S=1-85. DR PDB; 1YJN; X-ray; 3.00 A; S=1-85. DR PDB; 1YJW; X-ray; 2.90 A; S=1-85. DR PDB; 2OTJ; X-ray; 2.90 A; S=1-85. DR PDB; 2OTL; X-ray; 2.70 A; S=1-85. DR PDB; 2QA4; X-ray; 3.00 A; S=1-85. DR PDB; 2QEX; X-ray; 2.90 A; S=1-85. DR PDB; 3CC2; X-ray; 2.40 A; S=1-85. DR PDB; 3CC4; X-ray; 2.70 A; S=1-85. DR PDB; 3CC7; X-ray; 2.70 A; S=1-85. DR PDB; 3CCE; X-ray; 2.75 A; S=1-85. DR PDB; 3CCJ; X-ray; 2.70 A; S=1-85. DR PDB; 3CCL; X-ray; 2.90 A; S=1-85. DR PDB; 3CCM; X-ray; 2.55 A; S=1-85. DR PDB; 3CCQ; X-ray; 2.90 A; S=1-85. DR PDB; 3CCR; X-ray; 3.00 A; S=1-85. DR PDB; 3CCS; X-ray; 2.95 A; S=1-85. DR PDB; 3CCU; X-ray; 2.80 A; S=1-85. DR PDB; 3CCV; X-ray; 2.90 A; S=1-85. DR PDB; 3CD6; X-ray; 2.75 A; S=1-85. DR PDB; 3CMA; X-ray; 2.80 A; S=1-85. DR PDB; 3CME; X-ray; 2.95 A; S=1-85. DR PDB; 3CPW; X-ray; 2.70 A; R=1-85. DR PDB; 3CXC; X-ray; 3.00 A; R=2-85. DR PDB; 3G4S; X-ray; 3.20 A; S=2-82. DR PDB; 3G6E; X-ray; 2.70 A; S=2-82. DR PDB; 3G71; X-ray; 2.85 A; S=2-82. DR PDB; 3I55; X-ray; 3.11 A; S=1-85. DR PDB; 3I56; X-ray; 2.90 A; S=1-85. DR PDB; 3OW2; X-ray; 2.70 A; R=2-82. DR PDB; 4ADX; EM; 6.60 A; S=1-85. DR PDB; 4V4S; X-ray; 6.76 A; X=2-85. DR PDB; 4V4T; X-ray; 6.46 A; X=2-85. DR PDB; 4V9F; X-ray; 2.40 A; S=1-85. 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; 4V4S; -. DR PDBsum; 4V4T; -. DR PDBsum; 4V9F; -. DR SMR; P12732; -. DR STRING; 272569.rrnAC1609; -. DR EnsemblBacteria; AAV46526; AAV46526; rrnAC1609. DR GeneID; 40152575; -. DR KEGG; hma:rrnAC1609; -. DR PATRIC; fig|272569.17.peg.2299; -. DR eggNOG; arCOG04072; Archaea. DR eggNOG; COG0089; LUCA. DR HOGENOM; HOG000231364; -. DR KO; K02892; -. DR OMA; MDPYKVI; -. DR OrthoDB; 113971at2157; -. DR EvolutionaryTrace; P12732; -. DR Proteomes; UP000001169; Chromosome I. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR019985; Ribosomal_L23. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR TIGRFAMs; TIGR03636; uL23_arch; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3196689, FT ECO:0000269|PubMed:3350019}. FT CHAIN 2 85 50S ribosomal protein L23. FT /FTId=PRO_0000129435. FT STRAND 5 9 {ECO:0000244|PDB:1VQ8}. FT HELIX 13 21 {ECO:0000244|PDB:1VQ8}. FT STRAND 24 29 {ECO:0000244|PDB:1VQ8}. FT HELIX 35 46 {ECO:0000244|PDB:1VQ8}. FT STRAND 50 57 {ECO:0000244|PDB:1VQ8}. FT STRAND 61 69 {ECO:0000244|PDB:1VQ8}. FT STRAND 71 73 {ECO:0000244|PDB:1YJ9}. FT HELIX 75 79 {ECO:0000244|PDB:1VQ8}. SQ SEQUENCE 85 AA; 9602 MW; 2A2E869D640D5B60 CRC64; MSWDVIKHPH VTEKAMNDMD FQNKLQFAVD DRASKGEVAD AVEEQYDVTV EQVNTQNTMD GEKKAVVRLS EDDDAQEVAS RIGVF //