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Database: UniProt
Entry: RL9_GRABC
LinkDB: RL9_GRABC
Original site: RL9_GRABC 
ID   RL9_GRABC               Reviewed;         191 AA.
AC   Q0BPY8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Large ribosomal subunit protein bL9 {ECO:0000255|HAMAP-Rule:MF_00503};
DE   AltName: Full=50S ribosomal protein L9 {ECO:0000305};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503};
GN   OrderedLocusNames=GbCGDNIH1_2216;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI63114.1; -; Genomic_DNA.
DR   RefSeq; WP_011632916.1; NC_008343.2.
DR   AlphaFoldDB; Q0BPY8; -.
DR   SMR; Q0BPY8; -.
DR   STRING; 391165.GbCGDNIH1_2216; -.
DR   GeneID; 69746395; -.
DR   KEGG; gbe:GbCGDNIH1_2216; -.
DR   eggNOG; COG0359; Bacteria.
DR   HOGENOM; CLU_078938_1_0_5; -.
DR   OrthoDB; 9788336at2; -.
DR   Proteomes; UP000001963; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L9, C-terminal domain; 1.
DR   Gene3D; 3.40.5.10; Ribosomal protein L9, N-terminal domain; 1.
DR   HAMAP; MF_00503; Ribosomal_bL9; 1.
DR   InterPro; IPR000244; Ribosomal_bL9.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_bL9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_bL9_C.
DR   InterPro; IPR036791; Ribosomal_bL9_C_sf.
DR   InterPro; IPR020070; Ribosomal_bL9_N.
DR   InterPro; IPR036935; Ribosomal_bL9_N_sf.
DR   NCBIfam; TIGR00158; L9; 1.
DR   PANTHER; PTHR21368:SF18; 39S RIBOSOMAL PROTEIN L9, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21368; 50S RIBOSOMAL PROTEIN L9; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF55653; Ribosomal protein L9 C-domain; 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..191
FT                   /note="Large ribosomal subunit protein bL9"
FT                   /id="PRO_1000014784"
SQ   SEQUENCE   191 AA;  20631 MW;  D857D587E49DB75E CRC64;
     MAAVELILLQ RVEKLGQMGD LVRVKPGYAR NFLLPGGRAI RATKANTERF EQQRAQLEAQ
     NLKRREEAER IAERVSGLSV VIIRQAGESG GLYGSVSSRD IAVAITESGL SVNRQQIQLD
     QPIKMLGLTD VRVVLHPEVV LPVTVNVARS VEEAERQARG EAVGLAAEEA AAAAEAALIE
     VADEEEVEIS A
//
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