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RL13_DEIRA
ID   RL13_DEIRA              Reviewed;         174 AA.
AC   Q9RXY1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=50S ribosomal protein L13;
GN   Name=rplM; OrderedLocusNames=DR_0174;
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, PROTEIN SEQUENCE
RP   OF 1-5, AND CONTACTS WITH 23S RRNA.
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 is one of the early assembly proteins of the 50S
CC       ribosomal subunit (By similarity). Binds to the 23S rRNA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts proteins L3 and
CC       L20. {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 uL13 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF09760.1; -; Genomic_DNA.
DR   PIR; E75552; E75552.
DR   RefSeq; NP_293898.2; NC_001263.1.
DR   PDB; 1NKW; X-ray; 3.10 A; H=1-174.
DR   PDB; 1NWX; X-ray; 3.50 A; H=1-174.
DR   PDB; 1NWY; X-ray; 3.30 A; H=1-174.
DR   PDB; 1SM1; X-ray; 3.42 A; H=1-174.
DR   PDB; 1XBP; X-ray; 3.50 A; H=1-174.
DR   PDB; 2ZJP; X-ray; 3.70 A; G=1-174.
DR   PDB; 2ZJQ; X-ray; 3.30 A; G=1-174.
DR   PDB; 2ZJR; X-ray; 2.91 A; G=1-174.
DR   PDB; 3CF5; X-ray; 3.30 A; G=1-174.
DR   PDB; 3DLL; X-ray; 3.50 A; G=1-174.
DR   PDB; 3PIO; X-ray; 3.25 A; G=1-174.
DR   PDB; 3PIP; X-ray; 3.45 A; G=1-174.
DR   PDB; 4IO9; X-ray; 3.20 A; G=1-174.
DR   PDB; 4IOA; X-ray; 3.20 A; G=1-174.
DR   PDB; 4IOC; X-ray; 3.60 A; G=1-174.
DR   PDB; 4U67; X-ray; 3.65 A; G=1-174.
DR   PDB; 4V49; X-ray; 8.70 A; H=29-171.
DR   PDB; 4V4A; X-ray; 9.50 A; H=29-171.
DR   PDB; 4V4G; X-ray; 11.50 A; K=29-171.
DR   PDB; 4WFN; X-ray; 3.54 A; G=1-174.
DR   PDB; 5DM6; X-ray; 2.90 A; G=30-171.
DR   PDB; 5DM7; X-ray; 3.00 A; G=30-171.
DR   PDB; 5JVG; X-ray; 3.43 A; G=1-174.
DR   PDB; 5JVH; X-ray; 3.58 A; G=1-174.
DR   PDB; 7A0R; X-ray; 3.30 A; G=30-172.
DR   PDB; 7A0S; X-ray; 3.22 A; G=30-172.
DR   PDB; 7A18; X-ray; 3.40 A; G=30-171.
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; 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; Q9RXY1; -.
DR   SMR; Q9RXY1; -.
DR   IntAct; Q9RXY1; 1.
DR   STRING; 243230.DR_0174; -.
DR   EnsemblBacteria; AAF09760; AAF09760; DR_0174.
DR   KEGG; dra:DR_0174; -.
DR   PATRIC; fig|243230.17.peg.338; -.
DR   eggNOG; COG0102; Bacteria.
DR   HOGENOM; CLU_082184_2_2_0; -.
DR   InParanoid; Q9RXY1; -.
DR   OMA; DFVVIIN; -.
DR   OrthoDB; 1822215at2; -.
DR   EvolutionaryTrace; Q9RXY1; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00392; Ribosomal_L13; 1.
DR   Gene3D; 3.90.1180.10; -; 1.
DR   HAMAP; MF_01366; Ribosomal_L13; 1.
DR   InterPro; IPR005822; Ribosomal_L13.
DR   InterPro; IPR005823; Ribosomal_L13_bac-type.
DR   InterPro; IPR023563; Ribosomal_L13_CS.
DR   InterPro; IPR036899; Ribosomal_L13_sf.
DR   PANTHER; PTHR11545; PTHR11545; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   PIRSF; PIRSF002181; Ribosomal_L13; 1.
DR   SUPFAM; SSF52161; SSF52161; 1.
DR   TIGRFAMs; TIGR01066; rplM_bact; 1.
DR   PROSITE; PS00783; RIBOSOMAL_L13; 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..174
FT                   /note="50S ribosomal protein L13"
FT                   /id="PRO_0000133733"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:2ZJQ"
FT   HELIX           51..63
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:7A18"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:7A0R"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:7A0R"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           115..121
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           124..133
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           139..145
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:4IOA"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:7A18"
SQ   SEQUENCE   174 AA;  19190 MW;  9F7B977882CB715E CRC64;
     MAFPDTDVSP PRGGPSSPAK SPLLRSFKVK TYIPKNDEQN WVVVDASGVP LGRLATLIAS
     RIRGKHRPDF TPNMIQGDFV VVINAAQVAL TGKKLDDKVY TRYTGYQGGL KTETAREALS
     KHPERVIEHA VFGMLPKGRQ GRAMHTRLKV YAGETHPHSA QKPQVLKTQP LEVK
 
 
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