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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}.
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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
 
 
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