(data stored in ACNUC7421 zone)

SWISSPROT: RL22_LEGPC

ID   RL22_LEGPC              Reviewed;         111 AA.
AC   A5IHQ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, 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=LPC_3008;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000675; ABQ56909.1; -; Genomic_DNA.
DR   RefSeq; WP_010946083.1; NC_009494.2.
DR   SMR; A5IHQ9; -.
DR   EnsemblBacteria; ABQ56909; ABQ56909; LPC_3008.
DR   KEGG; lpc:LPC_3008; -.
DR   HOGENOM; HOG000205046; -.
DR   KO; K02890; -.
DR   OMA; KRIQPRA; -.
DR   BioCyc; LPNE400673:LPC_RS01940-MONOMER; -.
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;
DR   PRODOM; A5IHQ9.
DR   SWISS-2DPAGE; A5IHQ9.
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..111
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_1000052597"
SQ   SEQUENCE   111 AA;  12021 MW;  AE8606468BC27132 CRC64;
     MEVTAKLKGA PLSAQKGRLV ADMIRNMNVS GALDVLKFTP KKGAKLMLKL LESAIANAEN
     NNGADIDDLK VGMVCVDEAT TLKRISPRAK GRANRICKRT CHITIKVSDE E
//

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