RL25_STAHJ
ID RL25_STAHJ Reviewed; 221 AA.
AC Q4L3F8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=SH2510;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05819.1; -; Genomic_DNA.
DR RefSeq; WP_011276760.1; NC_007168.1.
DR AlphaFoldDB; Q4L3F8; -.
DR SMR; Q4L3F8; -.
DR STRING; 279808.SH2510; -.
DR EnsemblBacteria; BAE05819; BAE05819; SH2510.
DR KEGG; sha:SH2510; -.
DR eggNOG; COG1825; Bacteria.
DR HOGENOM; CLU_075939_2_1_9; -.
DR OMA; HVDFYEV; -.
DR OrthoDB; 1673077at2; -.
DR Proteomes; UP000000543; 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..221
FT /note="50S ribosomal protein L25"
FT /id="PRO_0000181600"
FT REGION 174..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 24282 MW; 1F791FFF53A08631 CRC64;
MASLKSIIRQ GKQTRSDLKK LRNTGKVPAV VYGYGTKNTS VKVDEVEFIK VIREVGRNGV
IDLGVGSKSI KVMVSDYQFD PLKNQITHID FLAINMTEER TVDVPVHLVG EAAGAKEGGV
VEQPLFDLQV TATPENIPES IEVDITELEV NDSYSVSDIK VSGDFTIEND PEESVVTVVP
PTDEPTEEEV EAMEGEAATE EPEVVGEEKE EDSEEENKDE E