ID   RL22_MESH2              Reviewed;         203 AA.
AC   Q601K9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=mhp193;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27449.1; -; Genomic_DNA.
DR   RefSeq; WP_011206030.1; NC_006360.1.
DR   AlphaFoldDB; Q601K9; -.
DR   SMR; Q601K9; -.
DR   STRING; 295358.mhp193; -.
DR   EnsemblBacteria; AAV27449; AAV27449; mhp193.
DR   KEGG; mhy:mhp193; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_1545931_0_0_14; -.
DR   OMA; RTSHFKV; -.
DR   PhylomeDB; Q601K9; -.
DR   Proteomes; UP000006822; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..203
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000243170"
FT   REGION          116..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  21976 MW;  DB7BD7206EAC340D CRC64;
     MKVENHNLAV ASLKTQRISA FKARLVAVLL KGKKVSDALA ILAHTKKKAS PIFTKLINSA
     VANAINNHGF EHSNLIIKAA IVNEGPTLKR FRPRAKGAAS QILKRTSHFK VILASQNGGE
     SQNQEYQEAE KNLVSKSPEN TQSGALSQQI RGEQPQNDPE NGVDSQLSAK TNSTTTAKKT
     DLADNNTKND ATNTVLAQEK EVK