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Database: UniProt
Entry: A0A0B6WXZ5_9BACT
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ID   A0A0B6WXZ5_9BACT        Unreviewed;       137 AA.
AC   A0A0B6WXZ5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=PYK22_02140 {ECO:0000313|EMBL:CDM66128.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66128.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM66128.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66128.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM66128.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66128.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CBXV010000007; CDM66128.1; -; Genomic_DNA.
DR   RefSeq; WP_041977040.1; NZ_CBXV010000007.1.
DR   AlphaFoldDB; A0A0B6WXZ5; -.
DR   STRING; 454194.PYK22_02140; -.
DR   OrthoDB; 9810939at2; -.
DR   Proteomes; UP000031518; 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   Reference proteome {ECO:0000313|Proteomes:UP000031518};
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}.
FT   REGION          114..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15405 MW;  A9D838953ADAE53B CRC64;
     MAKKTRAEIR EAIHRRIRRR VRGTAERPRL AIFRSAKHIY AQIINDDEGR TLAAASTLDP
     ELRGKLNGAG KIDAARAVGR LIAERALAKG IERVVFDRGG YRYHGRVKAL ADAAREAGLN
     KDEKRRERRE KPQAEAA
//
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