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Database: UniProt
Entry: G2FTW5_9FIRM
LinkDB: G2FTW5_9FIRM
Original site: G2FTW5_9FIRM 
ID   G2FTW5_9FIRM            Unreviewed;       148 AA.
AC   G2FTW5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Large ribosomal subunit protein bL9 {ECO:0000256|ARBA:ARBA00035292, ECO:0000256|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000256|HAMAP-Rule:MF_00503,
GN   ECO:0000313|EMBL:EGW38995.1};
GN   ORFNames=DOT_3175 {ECO:0000313|EMBL:EGW38995.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW38995.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW38995.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW38995.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00503}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000256|ARBA:ARBA00010605, ECO:0000256|HAMAP-Rule:MF_00503}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGW38995.1}.
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DR   EMBL; AGAF01000148; EGW38995.1; -; Genomic_DNA.
DR   RefSeq; WP_009619672.1; NZ_AGAF01000148.1.
DR   AlphaFoldDB; G2FTW5; -.
DR   PATRIC; fig|913865.3.peg.2908; -.
DR   eggNOG; COG0359; Bacteria.
DR   OrthoDB; 9788336at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
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_L9; 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   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00503}.
FT   DOMAIN          13..40
FT                   /note="Ribosomal protein L9"
FT                   /evidence="ECO:0000259|PROSITE:PS00651"
SQ   SEQUENCE   148 AA;  16434 MW;  830D4A57FF282377 CRC64;
     MKVILQVDVK GTGKKGQVLE VADGFARNFL FPKKLAIEAT TGNIQDISHK KELEDRRKEK
     EKVDAIELGG KLNALLIEVK TKTGEGGRLF GSVTNKEIVD ALKKQHGFEV DKRKLDIKEP
     IKALGNYEVH VKIHPEVTAK LQVKVVAI
//
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