RL25_ROSS1
ID RL25_ROSS1 Reviewed; 218 AA.
AC A5UQF4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
GN OrderedLocusNames=RoseRS_0426;
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000686; ABQ88857.1; -; Genomic_DNA.
DR RefSeq; WP_011955214.1; NC_009523.1.
DR AlphaFoldDB; A5UQF4; -.
DR SMR; A5UQF4; -.
DR STRING; 357808.RoseRS_0426; -.
DR EnsemblBacteria; ABQ88857; ABQ88857; RoseRS_0426.
DR KEGG; rrs:RoseRS_0426; -.
DR eggNOG; COG1825; Bacteria.
DR HOGENOM; CLU_075939_0_1_0; -.
DR OMA; HVDFYEV; -.
DR OrthoDB; 1673077at2; -.
DR Proteomes; UP000006554; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..218
FT /note="50S ribosomal protein L25"
FT /id="PRO_1000142554"
FT REGION 185..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 23907 MW; EA5D2D6CC5F1BA10 CRC64;
MSEKFTLSLE PRSVLGKKVK RLRRSGILPA TVYGKGIEPI AVQIDARSFQ AIYRQAGRTS
LIELHIAGHP PLAAFIHALQ RHPVTRDIIH ADFRAVDLRQ EVEVAVPLHI EGKSPLVESG
EAVLNQVLST IEIRALPTAI PAHITVDISA LDSFDKSIHA RDLMLPPGVT LVTPGEELVV
GLAHTRAAEG EEEEAAAETP AEPELVRERR ESKEEEEE