RL23_HALMA
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 25-MAY-2022, entry version 154.
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}; OrderedLocusNames=rrnAC1609;
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 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 L31
RT from the archaebacterium Halobacterium marismortui.";
RL Eur. J. Biochem. 172:703-711(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7;
RA Arndt E., Kroemer W., Hatakeyama T.;
RT "Organization and nucleotide sequence of a gene cluster coding for eight
RT ribosomal proteins in the archaebacterium Halobacterium 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., 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 [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 ribosomes
RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT 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 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: Binds to a specific region on the 23S rRNA. Located at the
CC polypeptide exit tunnel on the outside of the subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein L29
CC and weakly with protein L39e. {ECO:0000255|HAMAP-Rule:MF_01369,
CC ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR EMBL; J05222; AAA86861.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46526.1; -; Genomic_DNA.
DR PIR; E35063; R5HS23.
DR RefSeq; WP_004591553.1; NZ_CP039138.1.
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; 1ML5; EM; 14.00 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; 4V42; X-ray; 5.50 A; BT=2-85.
DR PDB; 4V4R; X-ray; 5.90 A; BX=2-85.
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; 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; P12732; -.
DR SMR; P12732; -.
DR IntAct; P12732; 3.
DR STRING; 272569.rrnAC1609; -.
DR EnsemblBacteria; AAV46526; AAV46526; rrnAC1609.
DR GeneID; 40152575; -.
DR GeneID; 64821817; -.
DR KEGG; hma:rrnAC1609; -.
DR PATRIC; fig|272569.17.peg.2299; -.
DR eggNOG; arCOG04072; Archaea.
DR HOGENOM; CLU_037562_4_2_2; -.
DR OMA; MDPYKVI; -.
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 PANTHER; PTHR11620; PTHR11620; 1.
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; 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..85
FT /note="50S ribosomal protein L23"
FT /id="PRO_0000129435"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1YJ9"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 85 AA; 9602 MW; 2A2E869D640D5B60 CRC64;
MSWDVIKHPH VTEKAMNDMD FQNKLQFAVD DRASKGEVAD AVEEQYDVTV EQVNTQNTMD
GEKKAVVRLS EDDDAQEVAS RIGVF
