ID E8Q5Y2_BLOVB Unreviewed; 111 AA.
AC E8Q5Y2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331,
GN ECO:0000313|EMBL:ADV33598.1};
GN OrderedLocusNames=BVAF_197 {ECO:0000313|EMBL:ADV33598.1};
OS Blochmannia vafer (strain BVAF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=859654 {ECO:0000313|EMBL:ADV33598.1, ECO:0000313|Proteomes:UP000007464};
RN [1] {ECO:0000313|EMBL:ADV33598.1, ECO:0000313|Proteomes:UP000007464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVAF {ECO:0000313|EMBL:ADV33598.1,
RC ECO:0000313|Proteomes:UP000007464};
RX PubMed=21126349; DOI=10.1186/1471-2164-11-720;
RA Williams L.E., Wernegreen J.J.;
RT "Unprecedented loss of ammonia assimilation capability in a urease-encoding
RT bacterial mutualist.";
RL BMC Genomics 11:687-687(2010).
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:0000256|HAMAP-Rule:MF_01331}.
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. {ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004008}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004005}.
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DR EMBL; CP002189; ADV33598.1; -; Genomic_DNA.
DR RefSeq; WP_013516523.1; NC_014909.2.
DR AlphaFoldDB; E8Q5Y2; -.
DR STRING; 859654.BVAF_197; -.
DR KEGG; bva:BVAF_197; -.
DR HOGENOM; CLU_083987_3_3_6; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000007464; Chromosome.
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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR018260; Ribosomal_uL22_CS.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01044; rplV_bact; 1.
DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01331}.
SQ SEQUENCE 111 AA; 12696 MW; 26B6B034432568E6 CRC64;
MESMAKYRYI RSSAQKVRLV VNMIRGKYVS RALDILNYTN KKSAYVVKKT LESAIANAEH
NDGMNIDNLK IIKIFVDNGP SIKRIMPRAK GRSDRILKRT SHLTVVVSEE K
//
