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Database: UniProt
Entry: A8WB84_9MOLU
LinkDB: A8WB84_9MOLU
Original site: A8WB84_9MOLU 
ID   A8WB84_9MOLU            Unreviewed;       129 AA.
AC   A8WB84;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000313|EMBL:ABW88128.1};
GN   Synonyms=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
OS   Broccoli phytoplasma sp. br273.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX   NCBI_TaxID=480809 {ECO:0000313|EMBL:ABW88128.1};
RN   [1] {ECO:0000313|EMBL:ABW88128.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Br273 {ECO:0000313|EMBL:ABW88128.1};
RA   Duduk B., Bulajic A., Duduk N., Calari A., Paltrinieri S., Krstic B.,
RA   Bertaccini A.;
RT   "Identification of phytoplasmas belonging to aster yellows ribosomal group
RT   in vegetables in Serbia.";
RL   Bull. Insectology 60:341-342(2007).
RN   [2] {ECO:0000313|EMBL:ABW88128.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Br273 {ECO:0000313|EMBL:ABW88128.1};
RA   Duduk B., Calari A., Paltrinieri S., Duduk N., Bertaccini A.;
RT   "Multigene analysis for differentiation of aster yellows phytoplasmas
RT   infecting carrots in Serbia.";
RL   Ann. Appl. Biol. 154:219-229(2009).
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; EU215431; ABW88128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8WB84; -.
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; IPR018260; Ribosomal_uL22_CS.
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.
DR   PROSITE; PS00464; RIBOSOMAL_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   129 AA;  14255 MW;  F403C3BD52ED3EC2 CRC64;
     METKNAKAIA RKVSIAPRKA RLVVDLIRGK NIAQAQAILT FTPKVAAPVI LKLLNSAVSN
     AVNNLKLNRE QLYVKEVFVN EGLRLKRMFP RAKGSGDMIK KRTSHITLVI TSSTNLQTSK
     EEEQSGSKN
//
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