RL22_DEIRA
ID RL22_DEIRA Reviewed; 134 AA.
AC Q9RXJ7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L22;
GN Name=rplV; OrderedLocusNames=DR_0316;
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 [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 [2]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, AND PROTEIN
RP SEQUENCE OF 1-5.
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The globular domain of the protein is located by the
CC polypeptide exit tunnel on the outside of the subunit while an extended
CC beta-hairpin forms part of the wall of the tunnel. Forms a pair of
CC 'tweezers' with L32 that hold together two different domains of the 23S
CC rRNA. Interacts with the tunnel-blocking modified macrolide
CC azithromycin. Upon binding of the macrolide troleadomycin to the
CC ribosome, the tip of the beta-hairpin is displaced, which severely
CC restricts the tunnel. This and experiments in E.coli have led to the
CC suggestion that it is part of the gating mechanism involved in
CC translation arrest in the absence of the protein export system.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L32.
CC {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 universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF09897.1; -; Genomic_DNA.
DR PIR; D75534; D75534.
DR RefSeq; NP_294039.1; NC_001263.1.
DR RefSeq; WP_010886961.1; NZ_CP015081.1.
DR PDB; 1J5A; X-ray; 3.50 A; L=1-134.
DR PDB; 1JZX; X-ray; 3.10 A; L=1-134.
DR PDB; 1JZY; X-ray; 3.50 A; L=1-134.
DR PDB; 1JZZ; X-ray; 3.80 A; L=1-134.
DR PDB; 1K01; X-ray; 3.50 A; L=1-134.
DR PDB; 1NKW; X-ray; 3.10 A; Q=1-134.
DR PDB; 1NWX; X-ray; 3.50 A; Q=1-134.
DR PDB; 1NWY; X-ray; 3.30 A; Q=1-134.
DR PDB; 1OND; X-ray; 3.40 A; Q=1-134.
DR PDB; 1SM1; X-ray; 3.42 A; Q=1-134.
DR PDB; 1XBP; X-ray; 3.50 A; Q=1-134.
DR PDB; 2ZJP; X-ray; 3.70 A; P=1-134.
DR PDB; 2ZJQ; X-ray; 3.30 A; P=1-134.
DR PDB; 2ZJR; X-ray; 2.91 A; P=1-134.
DR PDB; 3CF5; X-ray; 3.30 A; P=1-134.
DR PDB; 3DLL; X-ray; 3.50 A; P=1-134.
DR PDB; 3PIO; X-ray; 3.25 A; P=1-134.
DR PDB; 3PIP; X-ray; 3.45 A; P=1-134.
DR PDB; 4IO9; X-ray; 3.20 A; P=1-134.
DR PDB; 4IOA; X-ray; 3.20 A; P=1-134.
DR PDB; 4IOC; X-ray; 3.60 A; P=1-134.
DR PDB; 4U67; X-ray; 3.65 A; P=1-134.
DR PDB; 4V49; X-ray; 8.70 A; Q=5-134.
DR PDB; 4V4A; X-ray; 9.50 A; Q=5-134.
DR PDB; 4V4G; X-ray; 11.50 A; T=5-134.
DR PDB; 4WFN; X-ray; 3.54 A; P=1-134.
DR PDB; 5DM6; X-ray; 2.90 A; P=8-134.
DR PDB; 5DM7; X-ray; 3.00 A; P=8-134.
DR PDB; 5JVG; X-ray; 3.43 A; P=1-134.
DR PDB; 5JVH; X-ray; 3.58 A; P=1-134.
DR PDB; 7A0R; X-ray; 3.30 A; P=6-133.
DR PDB; 7A0S; X-ray; 3.22 A; P=1-134.
DR PDB; 7A18; X-ray; 3.40 A; P=6-134.
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; 4WFN; -.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR PDBsum; 5JVG; -.
DR PDBsum; 5JVH; -.
DR PDBsum; 7A0R; -.
DR PDBsum; 7A0S; -.
DR PDBsum; 7A18; -.
DR AlphaFoldDB; Q9RXJ7; -.
DR SMR; Q9RXJ7; -.
DR IntAct; Q9RXJ7; 1.
DR STRING; 243230.DR_0316; -.
DR EnsemblBacteria; AAF09897; AAF09897; DR_0316.
DR KEGG; dra:DR_0316; -.
DR PATRIC; fig|243230.17.peg.482; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_083987_3_1_0; -.
DR InParanoid; Q9RXJ7; -.
DR OMA; KRIQPRA; -.
DR OrthoDB; 1666043at2; -.
DR EvolutionaryTrace; Q9RXJ7; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR PANTHER; PTHR13501; PTHR13501; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01044; rplV_bact; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..134
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125151"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2ZJQ"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3DLL"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4IO9"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:5DM6"
SQ SEQUENCE 134 AA; 15159 MW; 1AE12FA2D59FE944 CRC64;
MTAPEQTFRN KKQRKQQVKL RKPGFAVAKY VRMSPRKVRL VVDVIRGKSV QDAEDLLRFI
PRSASEPVAK VLNSAKANAL HNDEMLEDRL FVKEAYVDAG PTLKRLIPRA RGSANIIKKR
TSHITIIVAE KGNK
