RL22_BRUSU
ID RL22_BRUSU Reviewed; 129 AA.
AC Q8G080; Q075T9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
GN OrderedLocusNames=BR1228, BS1330_I1224;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=17014718; DOI=10.1186/1471-2180-6-84;
RA Halling S.M., Jensen A.E.;
RT "Intrinsic and selected resistance to antibiotics binding the ribosome:
RT analyses of Brucella 23S rrn, L4, L22, EF-Tu1, EF-Tu2, efflux and
RT phylogenetic implications.";
RL BMC Microbiol. 6:84-84(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
CC -!- FUNCTION: The globular domain of the protein is located near the
CC polypeptide exit tunnel on the outside of the subunit, while an
CC extended beta-hairpin is found that lines the wall of the exit tunnel
CC in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR EMBL; DQ227914; ABB77394.1; -; Genomic_DNA.
DR EMBL; AE014291; AAN30147.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18565.1; -; Genomic_DNA.
DR RefSeq; WP_004689764.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G080; -.
DR SMR; Q8G080; -.
DR EnsemblBacteria; AEM18565; AEM18565; BS1330_I1224.
DR GeneID; 45052263; -.
DR GeneID; 55590903; -.
DR KEGG; bms:BR1228; -.
DR KEGG; bsi:BS1330_I1224; -.
DR PATRIC; fig|204722.21.peg.2248; -.
DR HOGENOM; CLU_083987_3_0_5; -.
DR OMA; KRIQPRA; -.
DR PhylomeDB; Q8G080; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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 CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR PANTHER; PTHR13501; PTHR13501; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01044; rplV_bact; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..129
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125129"
SQ SEQUENCE 129 AA; 14085 MW; 937A6AA72A17F4CA CRC64;
MGKAKAPRQL KDNEAKAVAR TLRVSPQKLN LVASMIRGKK VNAALADLTF SRKRIAGTVK
KTLESAIANA ENNHDLDVDA LIVAEAYVGK SIVMKRFHVR GRGRASRIEK PFSHLTIVVR
EVAEKGEAA