RL25_DESAL
ID RL25_DESAL Reviewed; 218 AA.
AC B8FLB8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Dalk_3375;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL05064.1; -; Genomic_DNA.
DR RefSeq; WP_015948121.1; NC_011768.1.
DR AlphaFoldDB; B8FLB8; -.
DR SMR; B8FLB8; -.
DR EnsemblBacteria; ACL05064; ACL05064; Dalk_3375.
DR KEGG; dal:Dalk_3375; -.
DR eggNOG; COG1825; Bacteria.
DR HOGENOM; CLU_075939_2_1_7; -.
DR OMA; HVDFYEV; -.
DR OrthoDB; 1673077at2; -.
DR Proteomes; UP000000739; 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_1000142514"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 23364 MW; 736FFBF47711DC7C CRC64;
MKTHELKASP RTTRGNGPAR ALRREGFIPA VLYGPDSEPI TLSVSHKDLS DILQGVGSSQ
VMFNLNIEGA DAPRKAMIKE LQTNVVSQRY LHADFYEISM DRKLHVMVPV VVEGKSKGME
EGGLLQVIRR ELEVICLPGD IPEEFVIDVT ELGIGEAVHL SDVPKGDAVE FPESADFTVV
TVVAPTAAAL PEEGEEGEEG EEGGEGGEAE GAEAASEE
