RL9_STAAS
ID RL9_STAAS Reviewed; 148 AA.
AC Q6GD75;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=SAS0015;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC {ECO:0000255|HAMAP-Rule:MF_00503}.
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DR EMBL; BX571857; CAG41787.1; -; Genomic_DNA.
DR RefSeq; WP_000864305.1; NC_002953.3.
DR AlphaFoldDB; Q6GD75; -.
DR SMR; Q6GD75; -.
DR KEGG; sas:SAS0015; -.
DR HOGENOM; CLU_078938_3_2_9; -.
DR OMA; MKIILTH; -.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.430.100; -; 1.
DR Gene3D; 3.40.5.10; -; 1.
DR HAMAP; MF_00503; Ribosomal_L9; 1.
DR InterPro; IPR000244; Ribosomal_L9.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR020594; Ribosomal_L9_bac/chp.
DR InterPro; IPR020069; Ribosomal_L9_C.
DR InterPro; IPR036791; Ribosomal_L9_C_sf.
DR InterPro; IPR020070; Ribosomal_L9_N.
DR InterPro; IPR036935; Ribosomal_L9_N_sf.
DR PANTHER; PTHR21368; PTHR21368; 1.
DR Pfam; PF03948; Ribosomal_L9_C; 1.
DR Pfam; PF01281; Ribosomal_L9_N; 1.
DR SUPFAM; SSF55653; SSF55653; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR TIGRFAMs; TIGR00158; L9; 1.
DR PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..148
FT /note="50S ribosomal protein L9"
FT /id="PRO_0000176679"
SQ SEQUENCE 148 AA; 16454 MW; 4F765624D45A5BA1 CRC64;
MKVIFTQDVK GKGKKGEVKE VPVGYANNFL LKKNYAVEAT PGNLKQLELQ KKRAKQERQQ
EIEDAKALKE TLSNIEVEVS AKTGEGGKLF GSVSTKQIAE ALKAQHDIKI DKRKMDLPNG
IHSLGYTNVP VKLDKEVEGT IRVHTVEQ