RL22_STAA8
ID RL22_STAA8 Reviewed; 117 AA.
AC Q2FW11;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
GN OrderedLocusNames=SAOUHSC_02507;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000253; ABD31525.1; -; Genomic_DNA.
DR RefSeq; WP_000387527.1; NZ_LS483365.1.
DR RefSeq; YP_500974.1; NC_007795.1.
DR PDB; 4WCE; X-ray; 3.53 A; P=1-117.
DR PDB; 4WF9; X-ray; 3.43 A; P=1-117.
DR PDB; 4WFA; X-ray; 3.39 A; P=1-117.
DR PDB; 4WFB; X-ray; 3.43 A; P=1-117.
DR PDB; 5HKV; X-ray; 3.66 A; P=1-117.
DR PDB; 5HL7; X-ray; 3.55 A; P=1-117.
DR PDB; 5LI0; EM; 3.80 A; V=1-112.
DR PDB; 5ND8; EM; 3.70 A; V=1-117.
DR PDB; 5ND9; EM; 3.70 A; V=1-117.
DR PDB; 5NRG; X-ray; 3.44 A; P=1-117.
DR PDB; 5TCU; EM; 3.90 A; L5=1-112.
DR PDB; 6DDD; EM; 3.10 A; E=1-116.
DR PDB; 6DDG; EM; 3.10 A; E=1-116.
DR PDB; 6HMA; EM; 2.65 A; Q=1-112.
DR PDB; 6SJ6; EM; 3.23 A; V=1-117.
DR PDB; 6WQN; EM; 2.90 A; E=1-117.
DR PDB; 6WQQ; EM; 3.10 A; E=1-117.
DR PDB; 6WRS; EM; 3.20 A; E=1-117.
DR PDB; 6WRU; EM; 3.10 A; E=1-117.
DR PDB; 6YEF; EM; 3.20 A; V=1-117.
DR PDB; 7NHL; EM; 3.10 A; V=1-117.
DR PDB; 7NHM; EM; 3.10 A; V=1-117.
DR PDBsum; 4WCE; -.
DR PDBsum; 4WF9; -.
DR PDBsum; 4WFA; -.
DR PDBsum; 4WFB; -.
DR PDBsum; 5HKV; -.
DR PDBsum; 5HL7; -.
DR PDBsum; 5LI0; -.
DR PDBsum; 5ND8; -.
DR PDBsum; 5ND9; -.
DR PDBsum; 5NRG; -.
DR PDBsum; 5TCU; -.
DR PDBsum; 6DDD; -.
DR PDBsum; 6DDG; -.
DR PDBsum; 6HMA; -.
DR PDBsum; 6SJ6; -.
DR PDBsum; 6WQN; -.
DR PDBsum; 6WQQ; -.
DR PDBsum; 6WRS; -.
DR PDBsum; 6WRU; -.
DR PDBsum; 6YEF; -.
DR PDBsum; 7NHL; -.
DR PDBsum; 7NHM; -.
DR AlphaFoldDB; Q2FW11; -.
DR SMR; Q2FW11; -.
DR IntAct; Q2FW11; 2.
DR STRING; 1280.SAXN108_2494; -.
DR EnsemblBacteria; ABD31525; ABD31525; SAOUHSC_02507.
DR GeneID; 3920883; -.
DR GeneID; 58091471; -.
DR GeneID; 66840457; -.
DR KEGG; sao:SAOUHSC_02507; -.
DR PATRIC; fig|93061.5.peg.2262; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_083987_3_3_9; -.
DR OMA; KRIQPRA; -.
DR PRO; PR:Q2FW11; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..117
FT /note="50S ribosomal protein L22"
FT /id="PRO_1000052658"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:6HMA"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:6HMA"
FT TURN 22..26
FT /evidence="ECO:0007829|PDB:6WQN"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6DDD"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:6HMA"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6WQN"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6HMA"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6WQN"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:6HMA"
SQ SEQUENCE 117 AA; 12835 MW; 98D1E37BEE51DE4B CRC64;
MEAKAVARTI RIAPRKVRLV LDLIRGKNAA EAIAILKLTN KASSPVIEKV LMSALANAEH
NYDMNTDELV VKEAYANEGP TLKRFRPRAQ GRASAINKRT SHITIVVSDG KEEAKEA