ID   RL25_STACT              Reviewed;         214 AA.
AC   B9DLD8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Sca_0151;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL27064.1; -; Genomic_DNA.
DR   RefSeq; WP_012664179.1; NC_012121.1.
DR   AlphaFoldDB; B9DLD8; -.
DR   SMR; B9DLD8; -.
DR   STRING; 396513.SCA_0151; -.
DR   PRIDE; B9DLD8; -.
DR   GeneID; 60546168; -.
DR   KEGG; sca:SCA_0151; -.
DR   eggNOG; COG1825; Bacteria.
DR   HOGENOM; CLU_075939_2_1_9; -.
DR   OMA; HVDFYEV; -.
DR   OrthoDB; 1673077at2; -.
DR   BioCyc; SCAR396513:SCA_RS00730-MON; -.
DR   Proteomes; UP000000444; 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..214
FT                   /note="50S ribosomal protein L25"
FT                   /id="PRO_1000166182"
FT   REGION          179..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..214
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  23192 MW;  FF878D8B6012DBBB CRC64;
     MASLKSIIRQ GKQRRSDLTA IRNSGKVPAV MYGYGQKNVS VKVDEVEFIK VIREVGRNGV
     IDLGVGSKTI KVMVADYQFD PLKNQITHID FLAINMSEER TVEVPVHLVG EAVGAKEGGV
     VDQPLFNLEV TATPENIPEY LEVEISGLEI GDSLSVADLN TTGDFTIENE PEATVVTVVP
     PTQGPSEAEI EEVEAGDADT PEPEVVGEKE EDEE