ID   RL22_PORGI              Reviewed;         134 AA.
AC   Q7MTL8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=PG_1933;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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=AAQ66914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015924; AAQ66914.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004583593.1; NC_002950.2.
DR   AlphaFoldDB; Q7MTL8; -.
DR   SMR; Q7MTL8; -.
DR   STRING; 242619.PG_1933; -.
DR   EnsemblBacteria; AAQ66914; AAQ66914; PG_1933.
DR   GeneID; 57239591; -.
DR   KEGG; pgi:PG_1933; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_083987_3_1_10; -.
DR   OMA; KRIQPRA; -.
DR   OrthoDB; 1666043at2; -.
DR   Proteomes; UP000000588; 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..134
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000125199"
SQ   SEQUENCE   134 AA;  15327 MW;  42B1466423AB1E8F CRC64;
     MGARKHNSAE ARKEALKQMY FAKLRNVPTS PRKMRLVADM IRGMEVNRAL GVLKFSNKEA
     SARVEKLLRS AVANWEEKNE RKAEEGELFV SRICVDGAST LKRLRPAPQG RGYRIRKRSN
     HVTIYVDTLN NDNN