ID   RL9_EHRCR               Reviewed;         208 AA.
AC   Q2GHF2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=ECH_0310;
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000236; ABD45500.1; -; Genomic_DNA.
DR   RefSeq; WP_006011335.1; NC_007799.1.
DR   AlphaFoldDB; Q2GHF2; -.
DR   SMR; Q2GHF2; -.
DR   STRING; 205920.ECH_0310; -.
DR   EnsemblBacteria; ABD45500; ABD45500; ECH_0310.
DR   KEGG; ech:ECH_0310; -.
DR   eggNOG; COG0359; Bacteria.
DR   HOGENOM; CLU_078938_1_1_5; -.
DR   OMA; MKIILTH; -.
DR   OrthoDB; 1959318at2; -.
DR   Proteomes; UP000008320; 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.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..208
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_0000236520"
FT   REGION          168..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   208 AA;  23359 MW;  60E187D9710AABBB CRC64;
     MLSVILKESV RNLGKAGMVL KVKPGYARYL LTQKKAVRAT KENLKSLEEQ YLFIEKENLE
     KLEAAKVLKA SLEDEFLIIT RQAADDGKLF GSVTPKCISK LLSDKGYNIH YRNIFFYSVI
     KYIGEYVVNL ELHPDLVLPI TLYVVKNDLG AMQAQKLHAE KKRKIEEGKV EKGSCTEGES
     LELGSVDNDI NSGNVDSNES EKQDSVSE