RL22_BRUSI
ID RL22_BRUSI Reviewed; 127 AA.
AC B0CH27;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=BSUIS_A1277;
OS Brucella suis (strain ATCC 23445 / NCTC 10510).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=470137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23445 / NCTC 10510;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000911; ABY38328.1; -; Genomic_DNA.
DR RefSeq; WP_004690916.1; NC_010169.1.
DR AlphaFoldDB; B0CH27; -.
DR SMR; B0CH27; -.
DR EnsemblBacteria; ABY38328; ABY38328; BSUIS_A1277.
DR KEGG; bmt:BSUIS_A1277; -.
DR HOGENOM; CLU_083987_3_0_5; -.
DR OMA; KRIQPRA; -.
DR Proteomes; UP000008545; 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; 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.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..127
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000354449"
SQ SEQUENCE 127 AA; 13872 MW; 784C0EA70A3E8B7C CRC64;
MGKAKAPRQL KDNEAKAVAR TLRVSPQKLN LVASMIRGKK VNAALADLTF SRKRIAGTVK
KTLESAIANA ENNHDLDVDA LIVAEAYVGK SIVMKRFHVR GRASRIEKPF SHLTIVVREV
AEKGEAA