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RL19_DEIRA
ID   RL19_DEIRA              Reviewed;         166 AA.
AC   Q9RWB4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=50S ribosomal protein L19;
GN   Name=rplS; OrderedLocusNames=DR_0755;
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 is located at the 30S-50S ribosomal subunit
CC       interface and may play a role in the structure and function of the
CC       aminoacyl-tRNA binding site (By similarity). Binds the 23S rRNA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L3 and L14. {ECO:0000269|PubMed:11677599,
CC       ECO:0000269|PubMed:12535524, ECO:0000269|PubMed:12623020,
CC       ECO:0000269|PubMed:12665853, ECO:0000269|PubMed:15059283,
CC       ECO:0000269|PubMed:15554968}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF10334.1; -; Genomic_DNA.
DR   PIR; G75478; G75478.
DR   RefSeq; NP_294479.1; NC_001263.1.
DR   RefSeq; WP_010887401.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; N=1-166.
DR   PDB; 1NWX; X-ray; 3.50 A; N=1-166.
DR   PDB; 1NWY; X-ray; 3.30 A; N=1-166.
DR   PDB; 1SM1; X-ray; 3.42 A; N=1-166.
DR   PDB; 1XBP; X-ray; 3.50 A; N=1-166.
DR   PDB; 2ZJP; X-ray; 3.70 A; M=1-166.
DR   PDB; 2ZJQ; X-ray; 3.30 A; M=1-166.
DR   PDB; 2ZJR; X-ray; 2.91 A; M=1-166.
DR   PDB; 3CF5; X-ray; 3.30 A; M=1-166.
DR   PDB; 3DLL; X-ray; 3.50 A; M=1-166.
DR   PDB; 3PIO; X-ray; 3.25 A; M=1-166.
DR   PDB; 3PIP; X-ray; 3.45 A; M=1-166.
DR   PDB; 4IO9; X-ray; 3.20 A; M=1-166.
DR   PDB; 4IOA; X-ray; 3.20 A; M=1-166.
DR   PDB; 4IOC; X-ray; 3.60 A; M=1-166.
DR   PDB; 4U67; X-ray; 3.65 A; M=1-166.
DR   PDB; 4V49; X-ray; 8.70 A; N=2-126.
DR   PDB; 4V4A; X-ray; 9.50 A; N=2-126.
DR   PDB; 4V4G; X-ray; 11.50 A; Q=2-126.
DR   PDB; 4WFN; X-ray; 3.54 A; M=2-166.
DR   PDB; 5DM6; X-ray; 2.90 A; M=2-106.
DR   PDB; 5DM7; X-ray; 3.00 A; M=2-115.
DR   PDB; 5JVG; X-ray; 3.43 A; M=1-166.
DR   PDB; 5JVH; X-ray; 3.58 A; M=1-166.
DR   PDB; 7A0R; X-ray; 3.30 A; M=1-113.
DR   PDB; 7A0S; X-ray; 3.22 A; M=1-166.
DR   PDB; 7A18; X-ray; 3.40 A; M=2-119.
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; Q9RWB4; -.
DR   SMR; Q9RWB4; -.
DR   IntAct; Q9RWB4; 1.
DR   STRING; 243230.DR_0755; -.
DR   EnsemblBacteria; AAF10334; AAF10334; DR_0755.
DR   KEGG; dra:DR_0755; -.
DR   PATRIC; fig|243230.17.peg.935; -.
DR   eggNOG; COG0335; Bacteria.
DR   HOGENOM; CLU_103507_0_2_0; -.
DR   InParanoid; Q9RWB4; -.
DR   OMA; TITVYYE; -.
DR   OrthoDB; 1698718at2; -.
DR   EvolutionaryTrace; Q9RWB4; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.790; -; 1.
DR   HAMAP; MF_00402; Ribosomal_L19; 1.
DR   InterPro; IPR038657; L19_sf.
DR   InterPro; IPR001857; Ribosomal_L19.
DR   InterPro; IPR018257; Ribosomal_L19_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR15680; PTHR15680; 1.
DR   Pfam; PF01245; Ribosomal_L19; 1.
DR   PIRSF; PIRSF002191; Ribosomal_L19; 1.
DR   PRINTS; PR00061; RIBOSOMALL19.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01024; rplS_bact; 1.
DR   PROSITE; PS01015; RIBOSOMAL_L19; 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..166
FT                   /note="50S ribosomal protein L19"
FT                   /id="PRO_0000163448"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:7A18"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   STRAND          45..58
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:2ZJR"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:7A0S"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:7A18"
SQ   SEQUENCE   166 AA;  18316 MW;  1DA8E740601FFAF9 CRC64;
     MQTHIKINRG ELLRGIEQDH TRQLPDFRPG DTVRVDTKVR EGNRTRSQAF EGVVIAINGS
     GSRKSFTVRK ISFGEGVERV FPFASPLVNQ VTIVERGKVR RAKLYYLREL RGKAARIKSD
     RSRVMKDAAR AQQDKANASA SQAAAAQADV TVISAAPEVA PETQGE
 
 
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