RL25_ACIAC
ID RL25_ACIAC Reviewed; 210 AA.
AC A1TT74;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Aave_3611;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) 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; CP000512; ABM34162.1; -; Genomic_DNA.
DR RefSeq; WP_011796659.1; NC_008752.1.
DR AlphaFoldDB; A1TT74; -.
DR SMR; A1TT74; -.
DR STRING; 397945.Aave_3611; -.
DR EnsemblBacteria; ABM34162; ABM34162; Aave_3611.
DR KEGG; aav:Aave_3611; -.
DR eggNOG; COG1825; Bacteria.
DR HOGENOM; CLU_075939_0_1_4; -.
DR OMA; HVDFYEV; -.
DR OrthoDB; 1673077at2; -.
DR Proteomes; UP000002596; 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_01336; Ribosomal_L25; 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 InterPro; IPR020055; Ribosomal_L25_short.
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..210
FT /note="50S ribosomal protein L25"
FT /id="PRO_1000052860"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 22878 MW; 5E3697B59F493605 CRC64;
MNFVAFERAK QGTGASRRLR NSGKTPGIVY GGSAEPQLIE VDHNALWHAL KKEAFHSSVL
DMELAGKTSK VLLRDVQYHP YKQLVLHIDF QRVDEKTKLH MKVPLHFTGA EESPAVKIDK
CMVNPVATEL DVSCMPSDLP EFINVDLSKL EKGRSLHLKD IKLPRGVSPV VRGGQQNPVL
VSVVPPVAEV EAPAEGAAAP APAPAKKGKK
