RL32_HALMA
ID RL32_HALMA Reviewed; 241 AA.
AC P12736; Q5V1T9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=50S ribosomal protein L32e;
DE AltName: Full=Hl5;
GN Name=rpl32e; OrderedLocusNames=rrnAC1595;
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 2-32 AND 98-113.
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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 99-241.
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 protein L15. {ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family.
CC {ECO:0000305}.
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DR EMBL; X58395; CAA41288.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46513.1; -; Genomic_DNA.
DR PIR; S16539; R7HSH5.
DR RefSeq; WP_011223739.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; V=99-241.
DR PDB; 1JJ2; X-ray; 2.40 A; X=2-241.
DR PDB; 1K73; X-ray; 3.01 A; Z=2-241.
DR PDB; 1K8A; X-ray; 3.00 A; Z=2-241.
DR PDB; 1K9M; X-ray; 3.00 A; Z=2-241.
DR PDB; 1KC8; X-ray; 3.01 A; Z=2-241.
DR PDB; 1KD1; X-ray; 3.00 A; Z=2-241.
DR PDB; 1KQS; X-ray; 3.10 A; X=2-241.
DR PDB; 1M1K; X-ray; 3.20 A; Z=2-241.
DR PDB; 1M90; X-ray; 2.80 A; Z=2-241.
DR PDB; 1N8R; X-ray; 3.00 A; Z=2-241.
DR PDB; 1NJI; X-ray; 3.00 A; Z=2-241.
DR PDB; 1Q7Y; X-ray; 3.20 A; Z=2-241.
DR PDB; 1Q81; X-ray; 2.95 A; Z=2-241.
DR PDB; 1Q82; X-ray; 2.98 A; Z=2-241.
DR PDB; 1Q86; X-ray; 3.00 A; Z=2-241.
DR PDB; 1QVF; X-ray; 3.10 A; X=2-241.
DR PDB; 1QVG; X-ray; 2.90 A; X=2-241.
DR PDB; 1S72; X-ray; 2.40 A; Y=1-241.
DR PDB; 1VQ4; X-ray; 2.70 A; Y=1-241.
DR PDB; 1VQ5; X-ray; 2.60 A; Y=1-241.
DR PDB; 1VQ6; X-ray; 2.70 A; Y=1-241.
DR PDB; 1VQ7; X-ray; 2.50 A; Y=1-241.
DR PDB; 1VQ8; X-ray; 2.20 A; Y=1-241.
DR PDB; 1VQ9; X-ray; 2.40 A; Y=1-241.
DR PDB; 1VQK; X-ray; 2.30 A; Y=1-241.
DR PDB; 1VQL; X-ray; 2.30 A; Y=1-241.
DR PDB; 1VQM; X-ray; 2.30 A; Y=1-241.
DR PDB; 1VQN; X-ray; 2.40 A; Y=1-241.
DR PDB; 1VQO; X-ray; 2.20 A; Y=1-241.
DR PDB; 1VQP; X-ray; 2.25 A; Y=1-241.
DR PDB; 1W2B; X-ray; 3.50 A; X=2-241.
DR PDB; 1YHQ; X-ray; 2.40 A; Y=1-241.
DR PDB; 1YI2; X-ray; 2.65 A; Y=1-241.
DR PDB; 1YIJ; X-ray; 2.60 A; Y=1-241.
DR PDB; 1YIT; X-ray; 2.80 A; Y=1-241.
DR PDB; 1YJ9; X-ray; 2.90 A; Y=1-241.
DR PDB; 1YJN; X-ray; 3.00 A; Y=1-241.
DR PDB; 1YJW; X-ray; 2.90 A; Y=1-241.
DR PDB; 2OTJ; X-ray; 2.90 A; Y=1-241.
DR PDB; 2OTL; X-ray; 2.70 A; Y=1-241.
DR PDB; 2QA4; X-ray; 3.00 A; Y=1-241.
DR PDB; 2QEX; X-ray; 2.90 A; Y=1-241.
DR PDB; 3CC2; X-ray; 2.40 A; Y=1-241.
DR PDB; 3CC4; X-ray; 2.70 A; Y=1-241.
DR PDB; 3CC7; X-ray; 2.70 A; Y=1-241.
DR PDB; 3CCE; X-ray; 2.75 A; Y=1-241.
DR PDB; 3CCJ; X-ray; 2.70 A; Y=1-241.
DR PDB; 3CCL; X-ray; 2.90 A; Y=1-241.
DR PDB; 3CCM; X-ray; 2.55 A; Y=1-241.
DR PDB; 3CCQ; X-ray; 2.90 A; Y=1-241.
DR PDB; 3CCR; X-ray; 3.00 A; Y=1-241.
DR PDB; 3CCS; X-ray; 2.95 A; Y=1-241.
DR PDB; 3CCU; X-ray; 2.80 A; Y=1-241.
DR PDB; 3CCV; X-ray; 2.90 A; Y=1-241.
DR PDB; 3CD6; X-ray; 2.75 A; Y=1-241.
DR PDB; 3CMA; X-ray; 2.80 A; Y=1-240.
DR PDB; 3CME; X-ray; 2.95 A; Y=1-240.
DR PDB; 3CPW; X-ray; 2.70 A; X=1-241.
DR PDB; 3CXC; X-ray; 3.00 A; X=2-241.
DR PDB; 3G4S; X-ray; 3.20 A; Y=96-237.
DR PDB; 3G6E; X-ray; 2.70 A; Y=96-237.
DR PDB; 3G71; X-ray; 2.85 A; Y=96-237.
DR PDB; 3I55; X-ray; 3.11 A; Y=1-241.
DR PDB; 3I56; X-ray; 2.90 A; Y=1-241.
DR PDB; 3OW2; X-ray; 2.70 A; X=96-237.
DR PDB; 4ADX; EM; 6.60 A; Y=1-241.
DR PDB; 4V9F; X-ray; 2.40 A; Y=1-241.
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; 4V9F; -.
DR AlphaFoldDB; P12736; -.
DR SMR; P12736; -.
DR IntAct; P12736; 2.
DR STRING; 272569.rrnAC1595; -.
DR EnsemblBacteria; AAV46513; AAV46513; rrnAC1595.
DR GeneID; 40152560; -.
DR KEGG; hma:rrnAC1595; -.
DR PATRIC; fig|272569.17.peg.2284; -.
DR eggNOG; arCOG00781; Archaea.
DR HOGENOM; CLU_071479_0_0_2; -.
DR OMA; EGKPQFN; -.
DR EvolutionaryTrace; P12736; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00513; Ribosomal_L32_L32e; 1.
DR DisProt; DP00944; -.
DR HAMAP; MF_00810; Ribosomal_L32e; 1.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR001515; Ribosomal_L32e.
DR InterPro; IPR023654; Ribosomal_L32e_arc.
DR InterPro; IPR018263; Ribosomal_L32e_CS.
DR InterPro; IPR036351; Ribosomal_L32e_sf.
DR PANTHER; PTHR23413; PTHR23413; 1.
DR Pfam; PF01655; Ribosomal_L32e; 1.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM01393; Ribosomal_L32e; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52042; SSF52042; 1.
DR PROSITE; PS00580; RIBOSOMAL_L32E; 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..241
FT /note="50S ribosomal protein L32e"
FT /id="PRO_0000131148"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 26
FT /note="S -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="LS -> SL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2QA4"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1VQ9"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 241 AA; 26416 MW; F4FFF58DE34B3711 CRC64;
MADNEEDVEA EEEYTELTDI SGVGPSKAES LREAGFESVE DVRGADQSAL ADVSGIGNAL
AARIKADVGG LEVESETEAE VEEEGGEEAP DEDVETELQA RGLTEKTPDL SDEDARLLTQ
RHRVGKPQFN RQDHHKKKRV STSWRKPRGQ LSKQRRGIKG KGDTVEAGFR SPTAVRGKHP
SGFEEVRVHN VDDLEGVDGD TEAVRIASKV GARKRERIEE EAEDAGIRVL NPTYVEVEVS
E
