ID A0A0A7I4D1_9BIFI Unreviewed; 119 AA.
AC A0A0A7I4D1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN ORFNames=AH68_01805 {ECO:0000313|EMBL:AIZ13975.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ13975.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ13975.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ13975.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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; CP007456; AIZ13975.1; -; Genomic_DNA.
DR RefSeq; WP_003808026.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I4D1; -.
DR SMR; A0A0A7I4D1; -.
DR STRING; 1447716.AH68_01805; -.
DR GeneID; 69563245; -.
DR KEGG; bka:AH68_01805; -.
DR HOGENOM; CLU_083987_3_3_11; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000030625; 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 119 AA; 13314 MW; A432194367AF8F4D CRC64;
MEAKAIARHV RVTPRKARRM VDLIRGKKAT EAITILKFAP QDASLPVRKV LESAIANARV
KADKAGEPFR ENDLVVKETY VDEGVTLKRF RARAQGRAAR INKRTSHITV VVANKEGNR
//
