ID M1ZRW2_CLOBO Unreviewed; 119 AA.
AC M1ZRW2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000256|ARBA:ARBA00035197, ECO:0000256|HAMAP-Rule:MF_01337};
GN Name=rplR {ECO:0000256|HAMAP-Rule:MF_01337,
GN ECO:0000313|EMBL:EKN42532.1};
GN ORFNames=CFSAN001627_06109 {ECO:0000313|EMBL:EKN42532.1};
OS Clostridium botulinum CFSAN001627.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1232189 {ECO:0000313|EMBL:EKN42532.1, ECO:0000313|Proteomes:UP000011944};
RN [1] {ECO:0000313|EMBL:EKN42532.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42532.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Strain E.A., Brown E., Allard M.W., Gonzalez-Escalona N., Timme R.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EKN42532.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42532.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Timme R.E., Allard M., Luo Y., Strain E., Gonzalez-Escalona N., Brown E.;
RT "Diversity in Clostridium botulinum.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is one of the proteins that bind and probably mediate
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. {ECO:0000256|HAMAP-
CC Rule:MF_01337}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01337}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000256|ARBA:ARBA00007116, ECO:0000256|HAMAP-Rule:MF_01337}.
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:EKN42532.1}.
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DR EMBL; AMXI01000348; EKN42532.1; -; Genomic_DNA.
DR AlphaFoldDB; M1ZRW2; -.
DR SMR; M1ZRW2; -.
DR PATRIC; fig|1232189.3.peg.986; -.
DR Proteomes; UP000011944; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00432; Ribosomal_L18_L5e; 1.
DR Gene3D; 3.30.420.100; -; 1.
DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR InterPro; IPR005484; Ribosomal_uL18.
DR InterPro; IPR004389; Ribosomal_uL18_bac-type.
DR NCBIfam; TIGR00060; L18_bact; 1.
DR PANTHER; PTHR12899; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12899:SF3; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
DR SUPFAM; SSF53137; Translational machinery components; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01337}.
SQ SEQUENCE 119 AA; 13371 MW; 3C927A69B9C6AC1B CRC64;
MFKKNDRSQS RTRRHMRVRK KIFGTAERPR LSVYRSEKHI YAQLIDDVEG KTLVAASSSE
KGFDGVGSNK EGAKLVGKMV AEKALEKGLK KVVFDRGGFI YHGRIKELAE GAREAGLDF
//