ID Q2PME1_9MOLU Unreviewed; 124 AA.
AC Q2PME1;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rpl22 {ECO:0000313|EMBL:ABC49689.1};
GN Synonyms=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
OS Coconut lethal yellowing phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrIV (Coconut lethal yellows group).
OX NCBI_TaxID=37369 {ECO:0000313|EMBL:ABC49689.1};
RN [1] {ECO:0000313|EMBL:ABC49689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLY-Hon {ECO:0000313|EMBL:ABC49689.1};
RA Roca M.M., Castillo M.G., Harrison N.A., Oropeza C.;
RT "First report of 16SrIV group phytoplasmas associated with declining coyol
RT and coconut palms in Olancho, Honduras.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABO26527.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LY {ECO:0000313|EMBL:ABO26527.1};
RX PubMed=17766869; DOI=10.1099/ijs.0.65013-0;
RA Martini M., Lee I.M., Bottner K.D., Zhao Y., Botti S., Bertaccini A.,
RA Harrison N.A., Carraro L., Marcone C., Khan A.J., Osler R.;
RT "Ribosomal protein gene-based phylogeny for finer differentiation and
RT classification of phytoplasmas.";
RL Int. J. Syst. Evol. Microbiol. 57:2037-2051(2007).
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:0000256|HAMAP-Rule:MF_01331}.
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. {ECO:0000256|ARBA:ARBA00025084}.
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. {ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004008}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004005}.
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DR EMBL; DQ318238; ABC49689.1; -; Genomic_DNA.
DR EMBL; EF193382; ABO26527.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2PME1; -.
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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01044; rplV_bact; 1.
DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01331}.
SQ SEQUENCE 124 AA; 13747 MW; E036C9FECBEE84C8 CRC64;
MNVQAVAKQI SIAPRKARLV VDLIRGKAIK EAQAILMFTP KASSFVVLKL LKSAVSNAIN
NFSMKFENLY IKEIFVNEGI RLTRLMPRAK GKSDKIKKRT SCITIVVASK NLETKGDIIN
GSKE
//
