ID   RL22_META1              Reviewed;         210 AA.
AC   B3PMP2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=MARTH_orf438;
OS   Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=243272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=158L3-1;
RX   PubMed=18573899; DOI=10.1128/iai.00516-08;
RA   Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA   Loraine A.E.;
RT   "Genome of Mycoplasma arthritidis.";
RL   Infect. Immun. 76:4000-4008(2008).
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; CP001047; ACF07294.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PMP2; -.
DR   SMR; B3PMP2; -.
DR   STRING; 243272.MARTH_orf438; -.
DR   EnsemblBacteria; ACF07294; ACF07294; MARTH_orf438.
DR   KEGG; mat:MARTH_orf438; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_1308988_0_0_14; -.
DR   OMA; PKTHREN; -.
DR   OrthoDB; 1666043at2; -.
DR   Proteomes; UP000008812; 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..210
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000354496"
FT   REGION          123..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  22789 MW;  FD0132E6B3B25750 CRC64;
     MVQDIFSKSA VASVKAQRIS PRKARLVADL IRYKTATQAL IILQTTNKKA SGIILKLLNS
     AIANATNNNG LDATKLVVTE ILVNDGPTLK RYQPHSRGRA YPILKRTSHF FIRVSEVSLP
     SVNEMTSKET VKEPAKKPSA KVEKPAEAKA PKQETSTKKP TTTTESKPKT SKAPAQKQAA
     KVAKPAAEDT KKPVKKSTTT TKSTKKEGSK