RL15_HALMA
ID RL15_HALMA Reviewed; 165 AA.
AC P12737; Q5V1U4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=50S ribosomal protein L15;
DE AltName: Full=Hl9;
DE AltName: Full=Hmal15;
GN Name=rpl15; OrderedLocusNames=rrnAC1590;
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=1543743; DOI=10.1016/0167-4781(92)90474-e;
RA Arndt E.;
RT "The genes for ribosomal protein L15 and the protein equivalent to secY in
RT the archaebacterium Haloarcula (Halobacterium) marismortui.";
RL Biochim. Biophys. Acta 1130:113-116(1992).
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 2-155.
RX PubMed=2591382; DOI=10.1111/j.1432-1033.1989.tb15166.x;
RA Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.;
RT "Primary structures of five ribosomal proteins from the archaebacterium
RT Halobacterium marismortui and their structural relationships to eubacterial
RT and eukaryotic ribosomal proteins.";
RL Eur. J. Biochem. 185:685-693(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
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 [5]
RP PROTEIN SEQUENCE OF 2-32.
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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 the 23S rRNA.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC proteins L18e and L32e. {ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; X63127; CAA44837.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46508.1; -; Genomic_DNA.
DR EMBL; X58395; CAA41293.1; -; Genomic_DNA.
DR PIR; S22349; R6HS15.
DR RefSeq; WP_011223737.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; J=2-165.
DR PDB; 1JJ2; X-ray; 2.40 A; K=2-165.
DR PDB; 1K73; X-ray; 3.01 A; M=2-165.
DR PDB; 1K8A; X-ray; 3.00 A; M=2-165.
DR PDB; 1K9M; X-ray; 3.00 A; M=2-165.
DR PDB; 1KC8; X-ray; 3.01 A; M=2-165.
DR PDB; 1KD1; X-ray; 3.00 A; M=2-165.
DR PDB; 1KQS; X-ray; 3.10 A; K=2-165.
DR PDB; 1M1K; X-ray; 3.20 A; M=2-165.
DR PDB; 1M90; X-ray; 2.80 A; M=2-165.
DR PDB; 1ML5; EM; 14.00 A; o=2-165.
DR PDB; 1N8R; X-ray; 3.00 A; M=2-165.
DR PDB; 1NJI; X-ray; 3.00 A; M=2-165.
DR PDB; 1Q7Y; X-ray; 3.20 A; M=2-165.
DR PDB; 1Q81; X-ray; 2.95 A; M=2-165.
DR PDB; 1Q82; X-ray; 2.98 A; M=2-165.
DR PDB; 1Q86; X-ray; 3.00 A; M=2-165.
DR PDB; 1QVF; X-ray; 3.10 A; K=2-165.
DR PDB; 1QVG; X-ray; 2.90 A; K=2-165.
DR PDB; 1S72; X-ray; 2.40 A; L=1-165.
DR PDB; 1VQ4; X-ray; 2.70 A; L=1-165.
DR PDB; 1VQ5; X-ray; 2.60 A; L=1-165.
DR PDB; 1VQ6; X-ray; 2.70 A; L=1-165.
DR PDB; 1VQ7; X-ray; 2.50 A; L=1-165.
DR PDB; 1VQ8; X-ray; 2.20 A; L=1-165.
DR PDB; 1VQ9; X-ray; 2.40 A; L=1-165.
DR PDB; 1VQK; X-ray; 2.30 A; L=1-165.
DR PDB; 1VQL; X-ray; 2.30 A; L=1-165.
DR PDB; 1VQM; X-ray; 2.30 A; L=1-165.
DR PDB; 1VQN; X-ray; 2.40 A; L=1-165.
DR PDB; 1VQO; X-ray; 2.20 A; L=1-165.
DR PDB; 1VQP; X-ray; 2.25 A; L=1-165.
DR PDB; 1W2B; X-ray; 3.50 A; K=2-165.
DR PDB; 1YHQ; X-ray; 2.40 A; L=1-165.
DR PDB; 1YI2; X-ray; 2.65 A; L=1-165.
DR PDB; 1YIJ; X-ray; 2.60 A; L=1-165.
DR PDB; 1YIT; X-ray; 2.80 A; L=1-165.
DR PDB; 1YJ9; X-ray; 2.90 A; L=1-165.
DR PDB; 1YJN; X-ray; 3.00 A; L=1-165.
DR PDB; 1YJW; X-ray; 2.90 A; L=1-165.
DR PDB; 2OTJ; X-ray; 2.90 A; L=1-165.
DR PDB; 2OTL; X-ray; 2.70 A; L=1-165.
DR PDB; 2QA4; X-ray; 3.00 A; L=1-165.
DR PDB; 2QEX; X-ray; 2.90 A; L=1-165.
DR PDB; 3CC2; X-ray; 2.40 A; L=1-165.
DR PDB; 3CC4; X-ray; 2.70 A; L=1-165.
DR PDB; 3CC7; X-ray; 2.70 A; L=1-165.
DR PDB; 3CCE; X-ray; 2.75 A; L=1-165.
DR PDB; 3CCJ; X-ray; 2.70 A; L=1-165.
DR PDB; 3CCL; X-ray; 2.90 A; L=1-165.
DR PDB; 3CCM; X-ray; 2.55 A; L=1-165.
DR PDB; 3CCQ; X-ray; 2.90 A; L=1-165.
DR PDB; 3CCR; X-ray; 3.00 A; L=1-165.
DR PDB; 3CCS; X-ray; 2.95 A; L=1-165.
DR PDB; 3CCU; X-ray; 2.80 A; L=1-165.
DR PDB; 3CCV; X-ray; 2.90 A; L=1-165.
DR PDB; 3CD6; X-ray; 2.75 A; L=1-165.
DR PDB; 3CMA; X-ray; 2.80 A; L=1-165.
DR PDB; 3CME; X-ray; 2.95 A; L=1-165.
DR PDB; 3CPW; X-ray; 2.70 A; K=1-165.
DR PDB; 3CXC; X-ray; 3.00 A; K=2-165.
DR PDB; 3G4S; X-ray; 3.20 A; L=1-165.
DR PDB; 3G6E; X-ray; 2.70 A; L=1-165.
DR PDB; 3G71; X-ray; 2.85 A; L=1-165.
DR PDB; 3I55; X-ray; 3.11 A; L=1-165.
DR PDB; 3I56; X-ray; 2.90 A; L=1-165.
DR PDB; 3OW2; X-ray; 2.70 A; K=2-151.
DR PDB; 4ADX; EM; 6.60 A; L=1-165.
DR PDB; 4V42; X-ray; 5.50 A; BO=2-165.
DR PDB; 4V4R; X-ray; 5.90 A; P=2-165.
DR PDB; 4V4S; X-ray; 6.76 A; P=2-165.
DR PDB; 4V4T; X-ray; 6.46 A; P=2-165.
DR PDB; 4V9F; X-ray; 2.40 A; L=1-165.
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; P12737; -.
DR SMR; P12737; -.
DR IntAct; P12737; 3.
DR STRING; 272569.rrnAC1590; -.
DR EnsemblBacteria; AAV46508; AAV46508; rrnAC1590.
DR GeneID; 40152555; -.
DR KEGG; hma:rrnAC1590; -.
DR PATRIC; fig|272569.17.peg.2279; -.
DR eggNOG; arCOG00779; Archaea.
DR HOGENOM; CLU_109163_0_0_2; -.
DR OMA; WGRVGQH; -.
DR EvolutionaryTrace; P12737; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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; 4.10.990.10; -; 1.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR027386; Rbsml_prot_L15/27a_N.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 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:2591382,
FT ECO:0000269|PubMed:3196689"
FT CHAIN 2..165
FT /note="50S ribosomal protein L15"
FT /id="PRO_0000104860"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="T -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..32
FT /note="RG -> NR (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3CCQ"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1JJ2"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1YIJ"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1VQO"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 32..40
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3CCM"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:1VQ7"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 165 AA; 17973 MW; AAF4318ADF0D8879 CRC64;
MTSKKKRQRG SRTHGGGSHK NRRGAGHRGG RGDAGRDKHE FHNHEPLGKS GFKRPQKVQE
EAATIDVREI DENVTLLAAD DVAEVEDGGF RVDVRDVVEE ADDADYVKVL GAGQVRHELT
LIADDFSEGA REKVEGAGGS VELTDLGEER QAEAEETEDA DADEE
