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Database: UniProt
Entry: A0A1J6WM80_9BACI
LinkDB: A0A1J6WM80_9BACI
Original site: A0A1J6WM80_9BACI 
ID   A0A1J6WM80_9BACI        Unreviewed;       120 AA.
AC   A0A1J6WM80;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=BHE18_00880 {ECO:0000313|EMBL:OIU72904.1};
OS   Rossellomorea aquimaris.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU72904.1, ECO:0000313|Proteomes:UP000182062};
RN   [1] {ECO:0000313|EMBL:OIU72904.1, ECO:0000313|Proteomes:UP000182062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAMM {ECO:0000313|EMBL:OIU72904.1,
RC   ECO:0000313|Proteomes:UP000182062};
RA   Waghmode S.R., Suryavanshi M.V.;
RT   "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT   biosurfactant production capacities.";
RL   Submitted (SEP-2016) 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:OIU72904.1}.
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DR   EMBL; MINN01000066; OIU72904.1; -; Genomic_DNA.
DR   RefSeq; WP_071617125.1; NZ_MINN01000066.1.
DR   AlphaFoldDB; A0A1J6WM80; -.
DR   OrthoDB; 9810939at2; -.
DR   Proteomes; UP000182062; 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:UP000182062};
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          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  13239 MW;  E94BE1A12A79B8CB CRC64;
     MITKPDKNKT RKKRHARVRS KITGTETRPR LNVFRSNKNI YAQIIDDMNG VTLASASSKD
     KDFGLESTAT VDAAAKVGEL VAKRAAEKGV KSVVFDRGGY LYHGRIKALA ESARENGLEF
//
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