RL9_HERAR
ID RL9_HERAR Reviewed; 150 AA.
AC A4G709;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; OrderedLocusNames=HEAR2159;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(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; CU207211; CAL62296.1; -; Genomic_DNA.
DR RefSeq; WP_011871568.1; NC_009138.1.
DR AlphaFoldDB; A4G709; -.
DR SMR; A4G709; -.
DR STRING; 204773.HEAR2159; -.
DR EnsemblBacteria; CAL62296; CAL62296; HEAR2159.
DR KEGG; har:HEAR2159; -.
DR eggNOG; COG0359; Bacteria.
DR HOGENOM; CLU_078938_4_1_4; -.
DR OMA; MKIILTH; -.
DR OrthoDB; 1959318at2; -.
DR Proteomes; UP000006697; 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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..150
FT /note="50S ribosomal protein L9"
FT /id="PRO_1000014791"
SQ SEQUENCE 150 AA; 15999 MW; 98771E1AB5AE35BB CRC64;
MQVILLEKVV NLGNLGEIVK VKDGYARNFL IPQRKARRAT TAAVAEFEVK RAELEKIAAE
KLAASQAQGE KLTGQTVQIS QKSGVDGRLF GSVTNADIAV ALTKQGFAVE KAQVRMPTGP
LKVTGDHTVA VALHTDVVIE VTITIVGEHA