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RL22_MYCPN
ID   RL22_MYCPN              Reviewed;         159 AA.
AC   P75575;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=50S ribosomal protein L22;
GN   Name=rplV; OrderedLocusNames=MPN_170; ORFNames=MP661;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   ANTIBIOTIC RESISTANT VARIANTS.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=14742195; DOI=10.1128/aac.48.2.460-465.2004;
RA   Pereyre S., Guyot C., Renaudin H., Charron A., Bebear C., Bebear C.M.;
RT   "In vitro selection and characterization of resistance to macrolides and
RT   related antibiotics in Mycoplasma pneumoniae.";
RL   Antimicrob. Agents Chemother. 48:460-465(2004).
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:0000250}.
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:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The antibiotic resistant variants could harbor other changes
CC       as the whole genes were not sequenced. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB96309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00089; AAB96309.1; ALT_INIT; Genomic_DNA.
DR   PIR; S73987; S73987.
DR   RefSeq; NP_109858.1; NC_000912.1.
DR   RefSeq; WP_015344888.1; NC_000912.1.
DR   AlphaFoldDB; P75575; -.
DR   SMR; P75575; -.
DR   STRING; 272634.MPN_170; -.
DR   EnsemblBacteria; AAB96309; AAB96309; MPN_170.
DR   KEGG; mpn:MPN_170; -.
DR   PATRIC; fig|272634.6.peg.188; -.
DR   HOGENOM; CLU_083987_3_3_14; -.
DR   OMA; RTSHFKV; -.
DR   Proteomes; UP000000808; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Antibiotic resistance; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..159
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000125184"
FT   REGION          129..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         111..114
FT                   /note="Missing (after 48 telithromycin passages; confers
FT                   resistance to various antibiotics in combination with a 23S
FT                   rRNA mutation and protein L4 H70L)"
FT   VARIANT         112
FT                   /note="N -> R (requires 2 nucleotide substitutions, after
FT                   37 telithromycin passages; confers resistance to various
FT                   antibiotics in combination with R114T, a 23S rRNA mutation
FT                   and protein L4 H70L)"
FT   VARIANT         114
FT                   /note="R -> T (after 20 and 32 telithromycin passages;
FT                   confers resistance to various antibiotics in combination
FT                   with a 23S rRNA mutation with and without protein L4 H70L)"
SQ   SEQUENCE   159 AA;  17324 MW;  6E5C6B8F96BFCD02 CRC64;
     MIAFAKQFRV RISPQKARLV CQLIVGKKTA DAQNILSNTP KKAATLIAKL LNSAIANATN
     NHGMNGDALY VFECVANQGP SMKRTIPRAK GSSNMITKRS SNLVVKLSDN PNERQELIKQ
     QKALVKKRVE GQQKAKMARQ KAVTSVVKAP SKTQGGVQK
 
 
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