RL9_ACIB5
ID RL9_ACIB5 Reviewed; 148 AA.
AC B7IBC3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=AB57_2511;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ42620.1; -; Genomic_DNA.
DR RefSeq; WP_000382591.1; NC_011586.2.
DR PDB; 6V39; EM; 3.04 A; H=1-148.
DR PDB; 6V3A; EM; 2.82 A; H=1-148.
DR PDB; 6V3B; EM; 2.91 A; H=1-148.
DR PDB; 6V3D; EM; 2.95 A; H=1-148.
DR PDB; 7M4V; EM; 2.54 A; H=1-148.
DR PDB; 7M4W; EM; 2.55 A; H=1-148.
DR PDB; 7M4X; EM; 2.66 A; H=1-148.
DR PDB; 7M4Y; EM; 2.50 A; H=1-148.
DR PDB; 7M4Z; EM; 2.92 A; H=1-148.
DR PDB; 7RYF; EM; 2.65 A; H=1-148.
DR PDB; 7RYG; EM; 2.38 A; H=1-148.
DR PDB; 7RYH; EM; 2.43 A; H=1-148.
DR PDBsum; 6V39; -.
DR PDBsum; 6V3A; -.
DR PDBsum; 6V3B; -.
DR PDBsum; 6V3D; -.
DR PDBsum; 7M4V; -.
DR PDBsum; 7M4W; -.
DR PDBsum; 7M4X; -.
DR PDBsum; 7M4Y; -.
DR PDBsum; 7M4Z; -.
DR PDBsum; 7RYF; -.
DR PDBsum; 7RYG; -.
DR PDBsum; 7RYH; -.
DR AlphaFoldDB; B7IBC3; -.
DR SMR; B7IBC3; -.
DR IntAct; B7IBC3; 2.
DR GeneID; 60879024; -.
DR GeneID; 66396724; -.
DR KEGG; abn:AB57_2511; -.
DR HOGENOM; CLU_078938_4_1_6; -.
DR OMA; MKIILTH; -.
DR Proteomes; UP000007094; 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.
DR PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..148
FT /note="50S ribosomal protein L9"
FT /id="PRO_1000126851"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:7M4V"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 41..59
FT /evidence="ECO:0007829|PDB:7M4V"
SQ SEQUENCE 148 AA; 15781 MW; 2C41568B82263C96 CRC64;
MDVILLQRIK NLGKLGDKVS VKAGYGRNFL IPQGKAVAAT EANTAAFEAR RAELEKQEAE
VLAAAQARAE QLNEVNIVIT AKAGDEGKLF GSIGTRDIAD ALTNAGLTVD RAEVRLPNGA
LRHTGEFNIA IQLHHDVVAE VLVTIVSE
