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Database: UniProt
Entry: A0A1U7CPJ8_9BACT
LinkDB: A0A1U7CPJ8_9BACT
Original site: A0A1U7CPJ8_9BACT 
ID   A0A1U7CPJ8_9BACT        Unreviewed;       211 AA.
AC   A0A1U7CPJ8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:APW60857.1};
GN   ORFNames=BSF38_02349 {ECO:0000313|EMBL:APW60857.1};
OS   Paludisphaera borealis.
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Paludisphaera.
OX   NCBI_TaxID=1387353 {ECO:0000313|EMBL:APW60857.1, ECO:0000313|Proteomes:UP000186309};
RN   [1] {ECO:0000313|Proteomes:UP000186309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX4 {ECO:0000313|Proteomes:UP000186309};
RA   Ivanova A.;
RT   "Comparative genomics of four Isosphaeraceae planctomycetes: a common pool
RT   of plasmids and glycoside hydrolase genes.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP019082; APW60857.1; -; Genomic_DNA.
DR   RefSeq; WP_076345775.1; NZ_JARLII010000074.1.
DR   AlphaFoldDB; A0A1U7CPJ8; -.
DR   STRING; 1387353.BSF38_02349; -.
DR   KEGG; pbor:BSF38_02349; -.
DR   OrthoDB; 9788336at2; -.
DR   Proteomes; UP000186309; 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_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   Reference proteome {ECO:0000313|Proteomes:UP000186309};
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          70..97
FT                   /note="Ribosomal protein L9"
FT                   /evidence="ECO:0000259|PROSITE:PS00651"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  22886 MW;  C9A11F47EE44D93E CRC64;
     MAKTTQPKTS KAKSGTSGKA GSGAGQSAKG KIAPVGPPRQ PGVERRRDHP LRAKNGQLSV
     LLTHDVPHVG RPGELVKVKP GFARNYLLPQ GLATFATPHN LRIVEKHRQR LRELEEARRA
     DLLNLAAQIA QRSLTIEANA NEEGHLYGSV NADQIAATLH GEGFPITTEN IRIEGPLKDL
     GLYNIKVHLG QDIDTEVKLW VVPTHTDEAP V
//
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