ID   RL25_STAAW              Reviewed;         217 AA.
AC   Q7A1S4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334};
DE   AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334}; OrderedLocusNames=MW0456;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in the
CC       ribosome where it forms part of the central protuberance.
CC       {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA
CC       independently of L5 and L18. {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}.
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DR   EMBL; BA000033; BAB94321.1; -; Genomic_DNA.
DR   RefSeq; WP_000157650.1; NC_003923.1.
DR   AlphaFoldDB; Q7A1S4; -.
DR   SMR; Q7A1S4; -.
DR   EnsemblBacteria; BAB94321; BAB94321; BAB94321.
DR   GeneID; 66838782; -.
DR   KEGG; sam:MW0456; -.
DR   HOGENOM; CLU_075939_2_1_9; -.
DR   OMA; HVDFYEV; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR   Gene3D; 2.170.120.20; -; 1.
DR   Gene3D; 2.40.240.10; -; 1.
DR   HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR   InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR029751; Ribosomal_L25.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR020057; Ribosomal_L25_b-dom.
DR   InterPro; IPR037121; Ribosomal_L25_C.
DR   InterPro; IPR001021; Ribosomal_L25_long.
DR   Pfam; PF01386; Ribosomal_L25p; 1.
DR   Pfam; PF14693; Ribosomal_TL5_C; 1.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00731; bL25_bact_ctc; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..217
FT                   /note="50S ribosomal protein L25"
FT                   /id="PRO_0000181597"
FT   REGION          178..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  23788 MW;  1F6A316EA0A45108 CRC64;
     MASLKSIIRQ GKQTRSDLKQ LRKSGKVPAV VYGYGTKNVS VKVDEVEFIK VIREVGRNGV
     IELGVGSKTI KVMVADYQFD PLKNQITHID FLAINMSEER TVEVPVQLVG EAVGAKEGGV
     VEQPLFNLEV TATPDNIPEA IEVDITELNI NDSLTVADVK VTGDFKIEND SAESVVTVVA
     PTEEPTEEEI EAMEGEQQTE EPEVVGESKE DEEKTEE