ID A0A255ESD4_9ACTN Unreviewed; 221 AA.
AC A0A255ESD4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Large ribosomal subunit protein bL25 {ECO:0000256|HAMAP-Rule:MF_01334};
DE AltName: Full=General stress protein CTC {ECO:0000256|HAMAP-Rule:MF_01334};
GN Name=rplY {ECO:0000256|HAMAP-Rule:MF_01334};
GN Synonyms=ctc {ECO:0000256|HAMAP-Rule:MF_01334};
GN ORFNames=CGZ91_02285 {ECO:0000313|EMBL:OYN92352.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN92352.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN92352.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN92352.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_01334}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01334}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYN92352.1}.
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DR EMBL; NMVJ01000001; OYN92352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ESD4; -.
DR OrthoDB; 5242980at2; -.
DR Proteomes; UP000216300; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L25, beta domain; 1.
DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR020057; Ribosomal_bL25_b-dom.
DR InterPro; IPR037121; Ribosomal_bL25_C.
DR InterPro; IPR001021; Ribosomal_bL25_long.
DR InterPro; IPR029751; Ribosomal_L25_dom.
DR NCBIfam; TIGR00731; bL25_bact_ctc; 1.
DR PANTHER; PTHR33284; RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33284:SF1; RIBOSOMAL PROTEIN L25_GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01386; Ribosomal_L25p; 1.
DR Pfam; PF14693; Ribosomal_TL5_C; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000216300};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01334}.
FT DOMAIN 8..93
FT /note="Large ribosomal subunit protein bL25 L25"
FT /evidence="ECO:0000259|Pfam:PF01386"
FT DOMAIN 101..179
FT /note="Large ribosomal subunit protein bL25 beta"
FT /evidence="ECO:0000259|Pfam:PF14693"
FT REGION 184..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 23675 MW; DC77B3CCA0DC4729 CRC64;
MAVDIIQLPA TQRTEFGKGA ARRIRRDDKV PAVVYGHGTE PLHITLPGHE TQLALRNSNA
LVEVTVEGGN KTLALPKQVQ RDPITGFLEH VDFIIVRRDE KVVVDVTLSF VGEAEPEALV
SVDRNEISVE VPVIAIPESI EVSVEGLNVG DQIKAADLKL PADTVYQGED DDLIVAVNAA
PTADQLEEEL AEAEAEAGIE RDEPEADNGG EASGSKGDSE D
//
