ID A0A432Z4Q4_9GAMM Unreviewed; 110 AA.
AC A0A432Z4Q4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 18.
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:RUO72823.1};
GN ORFNames=CWI81_12645 {ECO:0000313|EMBL:RUO72823.1};
OS Idiomarina seosinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=281739 {ECO:0000313|EMBL:RUO72823.1, ECO:0000313|Proteomes:UP000287908};
RN [1] {ECO:0000313|EMBL:RUO72823.1, ECO:0000313|Proteomes:UP000287908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-SP19 {ECO:0000313|EMBL:RUO72823.1,
RC ECO:0000313|Proteomes:UP000287908};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUO72823.1}.
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DR EMBL; PIQF01000005; RUO72823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432Z4Q4; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000287908; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000287908};
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 110 AA; 12015 MW; 04B443C5214D1625 CRC64;
MEAIAKHQFA RVSAQKGRLV ADQIRGLPVE KALDILAYSP KAAAGLIKKV LESAIANAEH
NEGADIDELK IAKIFLDEGP TMKRIKPRAK GRADRIFKRT SHITVVVSDS
//
