位置:首页 > 蛋白库 > RL36_DEIRA
RL36_DEIRA
ID   RL36_DEIRA              Reviewed;          37 AA.
AC   Q9RSK0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=50S ribosomal protein L36;
GN   Name=rpmJ; OrderedLocusNames=DR_2124;
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: Binds the 23S rRNA.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P80256, ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P80256,
CC       ECO:0000305};
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit.
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 bacterial ribosomal protein bL36 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000513; AAF11674.1; -; Genomic_DNA.
DR   PIR; E75312; E75312.
DR   RefSeq; NP_295847.1; NC_001263.1.
DR   RefSeq; WP_010888755.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; 4=1-36.
DR   PDB; 1NWX; X-ray; 3.50 A; 4=1-37.
DR   PDB; 1NWY; X-ray; 3.30 A; 4=1-37.
DR   PDB; 1SM1; X-ray; 3.42 A; 4=1-37.
DR   PDB; 1XBP; X-ray; 3.50 A; 4=1-37.
DR   PDB; 2ZJP; X-ray; 3.70 A; 4=1-37.
DR   PDB; 2ZJQ; X-ray; 3.30 A; 4=1-37.
DR   PDB; 2ZJR; X-ray; 2.91 A; 4=1-37.
DR   PDB; 3CF5; X-ray; 3.30 A; 4=1-37.
DR   PDB; 3DLL; X-ray; 3.50 A; 4=1-37.
DR   PDB; 3PIO; X-ray; 3.25 A; 4=1-37.
DR   PDB; 3PIP; X-ray; 3.45 A; 4=1-37.
DR   PDB; 4IO9; X-ray; 3.20 A; 4=1-37.
DR   PDB; 4IOA; X-ray; 3.20 A; 4=1-37.
DR   PDB; 4IOC; X-ray; 3.60 A; 4=1-37.
DR   PDB; 4V49; X-ray; 8.70 A; 4=2-36.
DR   PDB; 4V4A; X-ray; 9.50 A; 4=2-36.
DR   PDB; 4V4G; X-ray; 11.50 A; 6=2-36.
DR   PDB; 4V4R; X-ray; 5.90 A; B9=1-36.
DR   PDB; 4V4S; X-ray; 6.76 A; B9=1-36.
DR   PDB; 4V4T; X-ray; 6.46 A; 9=1-36.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
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; 4V49; -.
DR   PDBsum; 4V4A; -.
DR   PDBsum; 4V4G; -.
DR   PDBsum; 4V4R; -.
DR   PDBsum; 4V4S; -.
DR   PDBsum; 4V4T; -.
DR   AlphaFoldDB; Q9RSK0; -.
DR   SMR; Q9RSK0; -.
DR   IntAct; Q9RSK0; 1.
DR   STRING; 243230.DR_2124; -.
DR   EnsemblBacteria; AAF11674; AAF11674; DR_2124.
DR   KEGG; dra:DR_2124; -.
DR   PATRIC; fig|243230.17.peg.2347; -.
DR   eggNOG; COG0257; Bacteria.
DR   HOGENOM; CLU_135723_6_2_0; -.
DR   InParanoid; Q9RSK0; -.
DR   OrthoDB; 2066169at2; -.
DR   EvolutionaryTrace; Q9RSK0; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   DisProt; DP02016; -.
DR   HAMAP; MF_00251; Ribosomal_L36; 1.
DR   InterPro; IPR000473; Ribosomal_L36.
DR   InterPro; IPR035977; Ribosomal_L36_sp.
DR   PANTHER; PTHR42888; PTHR42888; 1.
DR   Pfam; PF00444; Ribosomal_L36; 1.
DR   SUPFAM; SSF57840; SSF57840; 1.
DR   TIGRFAMs; TIGR01022; rpmJ_bact; 1.
DR   PROSITE; PS00828; RIBOSOMAL_L36; 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.
FT   CHAIN           1..37
FT                   /note="50S ribosomal protein L36"
FT                   /id="PRO_0000126180"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P80256, ECO:0000305"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P80256, ECO:0000305"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P80256, ECO:0000305"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P80256, ECO:0000305"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:3PIO"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:3PIO"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:4IO9"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:2ZJR"
SQ   SEQUENCE   37 AA;  4309 MW;  B13477853DD772ED CRC64;
     MKVRSSVKKM CDNCKVVRRH GRVLVICSNV KHKQRQG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024