ID   RL22_AMOA5              Reviewed;         143 AA.
AC   B3EUL8; C3L4E3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Aasi_0192;
GN   ORFNames=Aasi_1495;
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2;
RX   PubMed=20023027; DOI=10.1128/jb.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACP20860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001102; ACP20860.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044282709.1; NC_010830.1.
DR   AlphaFoldDB; B3EUL8; -.
DR   SMR; B3EUL8; -.
DR   STRING; 452471.Aasi_1495; -.
DR   EnsemblBacteria; ACP20860; ACP20860; Aasi_1495.
DR   KEGG; aas:Aasi_1495; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_2379905_0_0_10; -.
DR   OMA; KRIQPRA; -.
DR   OrthoDB; 1666043at2; -.
DR   Proteomes; UP000001227; 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; -; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..143
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_1000142223"
FT   REGION          124..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  16197 MW;  F704530FCEDADC2C CRC64;
     MEAVAKLRKS PITPRKMRLV ADLIRGVKAD KAFAILRNEP KKCAIYLEKL LLAAVASWQH
     KNQDIQLEDA ELYIKTIQVD SAGMLKRLQP APQGRAHRIR KRFNHVTLVV DNLVAYEKPV
     KNEEATADNR SNKKVKITDG TKS