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Database: UniProt
Entry: A0A2K8K6U3_9RHOB
LinkDB: A0A2K8K6U3_9RHOB
Original site: A0A2K8K6U3_9RHOB 
ID   A0A2K8K6U3_9RHOB        Unreviewed;       126 AA.
AC   A0A2K8K6U3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=BG454_04485 {ECO:0000313|EMBL:ATX65177.1};
OS   Rhodobaca barguzinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobaca.
OX   NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX65177.1, ECO:0000313|Proteomes:UP000228948};
RN   [1] {ECO:0000313|EMBL:ATX65177.1, ECO:0000313|Proteomes:UP000228948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA   Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT   "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT   alga05 Genome.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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; CP024899; ATX65177.1; -; Genomic_DNA.
DR   RefSeq; WP_071479245.1; NZ_SODJ01000011.1.
DR   AlphaFoldDB; A0A2K8K6U3; -.
DR   STRING; 441209.GCA_001870665_03629; -.
DR   KEGG; rbg:BG454_04485; -.
DR   OrthoDB; 9805969at2; -.
DR   Proteomes; UP000228948; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000228948};
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   126 AA;  14102 MW;  C1E2656C10982D49 CRC64;
     MGKETNPRRV AENEAMAKTR MLRTSPQKLN LVAAMIRGKK VDKALTDLTF SKKRIAGDVK
     KCLQSAIANA ENNHGLDVDE LVVAEAWVGK NLVMKRGRPR ARGRFGKIMK PFSELTIKVR
     QVEEQA
//
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