(data stored in ACNUC7421 zone)

SWISSPROT: RL18_ALCBS

ID   RL18_ALCBS              Reviewed;         116 AA.
AC   Q0VSI7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337};
GN   Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; OrderedLocusNames=ABO_0413;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: This is one of the proteins that binds and probably mediates
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01337}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01337}.
DR   EMBL; AM286690; CAL15861.1; -; Genomic_DNA.
DR   RefSeq; WP_011587701.1; NC_008260.1.
DR   SMR; Q0VSI7; -.
DR   STRING; 393595.ABO_0413; -.
DR   PRIDE; Q0VSI7; -.
DR   EnsemblBacteria; CAL15861; CAL15861; ABO_0413.
DR   KEGG; abo:ABO_0413; -.
DR   eggNOG; ENOG4105K4C; Bacteria.
DR   eggNOG; COG0256; LUCA.
DR   HOGENOM; HOG000248742; -.
DR   KO; K02881; -.
DR   OMA; NKQIYAQ; -.
DR   OrthoDB; 1963491at2; -.
DR   BioCyc; ABOR393595:ABO_RS02150-MONOMER; -.
DR   Proteomes; UP000008871; Chromosome.
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   HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR   InterPro; IPR005484; Ribosomal_L18.
DR   InterPro; IPR004389; Ribosomal_L18_bac-type.
DR   PANTHER; PTHR12899; PTHR12899; 1.
DR   Pfam; PF00861; Ribosomal_L18p; 1.
DR   TIGRFAMs; TIGR00060; L18_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0VSI7.
DR   SWISS-2DPAGE; Q0VSI7.
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..116
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_1000052983"
SQ   SEQUENCE   116 AA;  12812 MW;  63803DC8945314D0 CRC64;
     MKDKKVARLR RAKRTRLKIR ELGEVRLCVH RTPRHIYAQV ISAAGDQVLA SASTVEKDLR
     ADATGNADAA TKVGQIIAQR AKEAGIERVA FDRSGFKYHG RVKALADAAR ENGLEF
//

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