ID D8JGJ7_ACISD Unreviewed; 148 AA.
AC D8JGJ7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:ADI90151.1};
GN OrderedLocusNames=AOLE_06290 {ECO:0000313|EMBL:ADI90151.1};
OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI90151.1, ECO:0000313|Proteomes:UP000000392};
RN [1] {ECO:0000313|EMBL:ADI90151.1, ECO:0000313|Proteomes:UP000000392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16667 / KCTC 23045 / DR1
RC {ECO:0000313|Proteomes:UP000000392};
RX PubMed=20639327; DOI=10.1128/JB.00722-10;
RA Jung J., Baek J.H., Park W.;
RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT DR1.";
RL J. Bacteriol. 192:4794-4795(2010).
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; CP002080; ADI90151.1; -; Genomic_DNA.
DR RefSeq; WP_004700828.1; NZ_VEIV01000002.1.
DR AlphaFoldDB; D8JGJ7; -.
DR GeneID; 9381684; -.
DR KEGG; acd:AOLE_06290; -.
DR eggNOG; COG0359; Bacteria.
DR HOGENOM; CLU_078938_4_1_6; -.
DR OrthoDB; 9788336at2; -.
DR Proteomes; UP000000392; 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 Coiled coil {ECO:0000256|SAM:Coils};
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"
FT COILED 37..74
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 148 AA; 15795 MW; 635FA7649CC93C80 CRC64;
MDVILLQRIK NLGKLGDKVS VKAGYGRNFL IPQGKAVAAT EANTAAFEAR RAELEKQEAE
ILAAAQARAE QLNEVNIVIT AKAGDEGKLF GSIGTRDIAD ALTNAGLTVD RAEVRLPNGA
LRHTGEFNIA IQLHHDVVAE VLVTIVSE
//