RL32_DEIRA
ID RL32_DEIRA Reviewed; 60 AA.
AC P49228;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=50S ribosomal protein L32;
GN Name=rpmF; OrderedLocusNames=DR_2366;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KR1;
RA Narumi I., Watanabe H.;
RT "Identification of the rpmF gene encoding ribosomal protein L32 from
RT Deinococcus radiodurans.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, AND PROTEIN
RP SEQUENCE OF 1-6.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA Bartels H., Franceschi F., Yonath A.;
RT "High resolution structure of the large ribosomal subunit from a mesophilic
RT eubacterium.";
RL Cell 107:679-688(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11677599; DOI=10.1038/35101544;
RA Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R.,
RA Yonath A., Franceschi F.;
RT "Structural basis for the interaction of antibiotics with the peptidyl
RT transferase centre in eubacteria.";
RL Nature 413:814-821(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TRNA MIMICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12535524; DOI=10.1016/s1097-2765(03)00009-1;
RA Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R.,
RA Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M.,
RA Yonath A.;
RT "Structural basis of the ribosomal machinery for peptide bond formation,
RT translocation, and nascent chain progression.";
RL Mol. Cell 11:91-102(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP MODIFIED MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12623020; DOI=10.1016/s0969-2126(03)00022-4;
RA Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H.,
RA Zarivach R., Yonath A.;
RT "Structural basis for the antibiotic activity of ketolides and azalides.";
RL Structure 11:329-338(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TROLEANDOMYCIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12665853; DOI=10.1038/nsb915;
RA Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D.,
RA Yonath A.;
RT "Structural insight into the role of the ribosomal tunnel in cellular
RT regulation.";
RL Nat. Struct. Biol. 10:366-370(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15059283; DOI=10.1186/1741-7007-2-4;
RA Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.;
RT "Alterations at the peptidyl transferase centre of the ribosome induced by
RT the synergistic action of the streptogramins dalfopristin and
RT quinupristin.";
RL BMC Biol. 2:4-4(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TIAMULIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15554968; DOI=10.1111/j.1365-2958.2004.04346.x;
RA Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.;
RT "Inhibition of peptide bond formation by pleuromutilins: the structure of
RT the 50S ribosomal subunit from Deinococcus radiodurans in complex with
RT tiamulin.";
RL Mol. Microbiol. 54:1287-1294(2004).
CC -!- FUNCTION: Forms a cluster with L17 and L22, and with L22, a pair of
CC 'tweezers' that hold together all the domains of the 23S rRNA.
CC Interacts with the antibiotic troleandomycin which blocks the peptide
CC exit tunnel.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts proteins L17 and
CC L22. {ECO:0000269|PubMed:11677599, ECO:0000269|PubMed:12535524,
CC ECO:0000269|PubMed:12623020, ECO:0000269|PubMed:12665853,
CC ECO:0000269|PubMed:15059283, ECO:0000269|PubMed:15554968}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.
CC {ECO:0000305}.
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DR EMBL; D63900; BAA09939.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF11913.1; -; Genomic_DNA.
DR PIR; F75282; F75282.
DR RefSeq; NP_296087.1; NC_001263.1.
DR RefSeq; WP_010888992.1; NZ_CP015081.1.
DR PDB; 1J5A; X-ray; 3.50 A; M=1-60.
DR PDB; 1JZX; X-ray; 3.10 A; M=1-60.
DR PDB; 1JZY; X-ray; 3.50 A; M=1-60.
DR PDB; 1JZZ; X-ray; 3.80 A; M=1-60.
DR PDB; 1K01; X-ray; 3.50 A; M=1-60.
DR PDB; 1NKW; X-ray; 3.10 A; Z=1-60.
DR PDB; 1NWX; X-ray; 3.50 A; Z=2-60.
DR PDB; 1NWY; X-ray; 3.30 A; Z=2-60.
DR PDB; 1OND; X-ray; 3.40 A; Z=1-60.
DR PDB; 1SM1; X-ray; 3.42 A; Z=1-60.
DR PDB; 1XBP; X-ray; 3.50 A; Z=2-60.
DR PDB; 2ZJP; X-ray; 3.70 A; Y=1-60.
DR PDB; 2ZJQ; X-ray; 3.30 A; Z=1-60.
DR PDB; 2ZJR; X-ray; 2.91 A; Z=1-60.
DR PDB; 3CF5; X-ray; 3.30 A; Y=1-60.
DR PDB; 3DLL; X-ray; 3.50 A; Y=1-60.
DR PDB; 3PIO; X-ray; 3.25 A; Z=1-60.
DR PDB; 3PIP; X-ray; 3.45 A; Z=1-60.
DR PDB; 4IO9; X-ray; 3.20 A; Z=1-60.
DR PDB; 4IOA; X-ray; 3.20 A; Z=1-60.
DR PDB; 4IOC; X-ray; 3.60 A; Z=1-60.
DR PDB; 4U67; X-ray; 3.65 A; Z=1-60.
DR PDB; 4V49; X-ray; 8.70 A; Z=2-59.
DR PDB; 4V4A; X-ray; 9.50 A; Z=2-59.
DR PDB; 4V4G; X-ray; 11.50 A; 2=2-59.
DR PDB; 4V4R; X-ray; 5.90 A; B5=1-60.
DR PDB; 4V4S; X-ray; 6.76 A; B5=1-60.
DR PDB; 4V4T; X-ray; 6.46 A; 5=1-60.
DR PDB; 4WFN; X-ray; 3.54 A; Z=1-60.
DR PDB; 5DM6; X-ray; 2.90 A; Z=3-59.
DR PDB; 5DM7; X-ray; 3.00 A; Z=3-59.
DR PDB; 5JVG; X-ray; 3.43 A; Z=1-60.
DR PDB; 5JVH; X-ray; 3.58 A; Z=1-60.
DR PDB; 7A0R; X-ray; 3.30 A; Z=2-59.
DR PDB; 7A0S; X-ray; 3.22 A; Z=2-59.
DR PDB; 7A18; X-ray; 3.40 A; Z=3-59.
DR PDBsum; 1J5A; -.
DR PDBsum; 1JZX; -.
DR PDBsum; 1JZY; -.
DR PDBsum; 1JZZ; -.
DR PDBsum; 1K01; -.
DR PDBsum; 1NKW; -.
DR PDBsum; 1NWX; -.
DR PDBsum; 1NWY; -.
DR PDBsum; 1OND; -.
DR PDBsum; 1SM1; -.
DR PDBsum; 1XBP; -.
DR PDBsum; 2ZJP; -.
DR PDBsum; 2ZJQ; -.
DR PDBsum; 2ZJR; -.
DR PDBsum; 3CF5; -.
DR PDBsum; 3DLL; -.
DR PDBsum; 3PIO; -.
DR PDBsum; 3PIP; -.
DR PDBsum; 4IO9; -.
DR PDBsum; 4IOA; -.
DR PDBsum; 4IOC; -.
DR PDBsum; 4U67; -.
DR PDBsum; 4V49; -.
DR PDBsum; 4V4A; -.
DR PDBsum; 4V4G; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4WFN; -.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR PDBsum; 5JVG; -.
DR PDBsum; 5JVH; -.
DR PDBsum; 7A0R; -.
DR PDBsum; 7A0S; -.
DR PDBsum; 7A18; -.
DR AlphaFoldDB; P49228; -.
DR SMR; P49228; -.
DR IntAct; P49228; 1.
DR STRING; 243230.DR_2366; -.
DR DrugBank; DB13179; Troleandomycin.
DR EnsemblBacteria; AAF11913; AAF11913; DR_2366.
DR KEGG; dra:DR_2366; -.
DR PATRIC; fig|243230.17.peg.2600; -.
DR eggNOG; COG0333; Bacteria.
DR HOGENOM; CLU_129084_1_3_0; -.
DR InParanoid; P49228; -.
DR OMA; HRACRHC; -.
DR OrthoDB; 2092354at2; -.
DR EvolutionaryTrace; P49228; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00340; Ribosomal_L32; 1.
DR InterPro; IPR002677; Ribosomal_L32p.
DR InterPro; IPR044957; Ribosomal_L32p_bact.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR35534; PTHR35534; 1.
DR Pfam; PF01783; Ribosomal_L32p; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR TIGRFAMs; TIGR01031; rpmF_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..60
FT /note="50S ribosomal protein L32"
FT /id="PRO_0000172336"
FT ZN_FING 33..49
FT /note="C4-type"
FT /evidence="ECO:0000305"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4IO9"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5DM6"
SQ SEQUENCE 60 AA; 6792 MW; 23D9FAEA1A00BC0C CRC64;
MAKHPVPKKK TSKSKRDMRR SHHALTAPNL TECPQCHGKK LSHHICPNCG YYDGRQVLAV
