ID   RL9_SPHAL               Reviewed;         210 AA.
AC   Q1GRV8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=Sala_1902;
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF53614.1; -; Genomic_DNA.
DR   RefSeq; WP_011542191.1; NC_008048.1.
DR   AlphaFoldDB; Q1GRV8; -.
DR   SMR; Q1GRV8; -.
DR   STRING; 317655.Sala_1902; -.
DR   EnsemblBacteria; ABF53614; ABF53614; Sala_1902.
DR   KEGG; sal:Sala_1902; -.
DR   eggNOG; COG0359; Bacteria.
DR   HOGENOM; CLU_078938_1_0_5; -.
DR   OMA; MKIILTH; -.
DR   OrthoDB; 1959318at2; -.
DR   Proteomes; UP000006578; Chromosome.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..210
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_0000258490"
FT   REGION          172..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  22599 MW;  38FCF70E521FD31C CRC64;
     MEIILLERIE KLGGIGDVVT VKNGFARNYL LPNNKALRAN EANRKLFEAN RAKIEADNAE
     RRSEAEGRAK DIDGKQIVLI RQASNTGQLY GSVSVRDIVD ALAEDGVTGV TKSMVELERP
     IKSLGLVDVK VKLHPEVVVT VGVNVARSPD EAEMQSQGID VIAAMFEEEQ AEAAAAALEP
     DSEEEFEAAT PPSELAAEAS DEDADDAKEA