ID   RL22_AKKM8              Reviewed;         112 AA.
AC   B2UMT4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Amuc_0298;
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC   107961 / Muc;
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
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}.
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DR   EMBL; CP001071; ACD04140.1; -; Genomic_DNA.
DR   RefSeq; WP_012419355.1; NC_010655.1.
DR   AlphaFoldDB; B2UMT4; -.
DR   SMR; B2UMT4; -.
DR   STRING; 349741.Amuc_0298; -.
DR   EnsemblBacteria; ACD04140; ACD04140; Amuc_0298.
DR   GeneID; 60879776; -.
DR   KEGG; amu:Amuc_0298; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_083987_3_3_0; -.
DR   OMA; KRIQPRA; -.
DR   OrthoDB; 1666043at2; -.
DR   BioCyc; AMUC349741:G1GBX-340-MON; -.
DR   Proteomes; UP000001031; 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; IPR018260; Ribosomal_L22/L17_CS.
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.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..112
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_1000166037"
SQ   SEQUENCE   112 AA;  12341 MW;  81EE46849D5AE3A6 CRC64;
     MEVKAVYKYA RISAKKMRDV AQEIQGLSVS QATDILSYTP KKGAYLLNKT LKSALANAEN
     NAELSVDTLV VKSVMVDEGP TMRRTMPRAR GSANMIRKRT SHITVILADQ EG