(data stored in ACNUC7421 zone)

SWISSPROT: D6XVP3_BACIE

ID   D6XVP3_BACIE            Unreviewed;        96 AA.
AC   D6XVP3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000256|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000256|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=Bsel_0117 {ECO:0000313|EMBL:ADH97666.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97666.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97666.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA.
CC       One of the proteins that surrounds the polypeptide exit tunnel on
CC       the outside of the ribosome. Forms the main docking site for
CC       trigger factor binding to the ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29,
CC       and trigger factor when it is bound to the ribosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23
CC       family. {ECO:0000256|HAMAP-Rule:MF_01369}.
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DR   EMBL; CP001791; ADH97666.1; -; Genomic_DNA.
DR   RefSeq; WP_013171096.1; NC_014219.1.
DR   STRING; 439292.Bsel_0117; -.
DR   EnsemblBacteria; ADH97666; ADH97666; Bsel_0117.
DR   KEGG; bse:Bsel_0117; -.
DR   eggNOG; ENOG41080UE; Bacteria.
DR   eggNOG; COG0089; LUCA.
DR   HOGENOM; HOG000231366; -.
DR   KO; K02892; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
DR   BioCyc; BSEL439292:G1GLR-141-MONOMER; -.
DR   Proteomes; UP000000271; 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   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVP3.
DR   SWISS-2DPAGE; D6XVP3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01369};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01369,
KW   ECO:0000313|EMBL:ADH97666.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01369};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01369}.
SQ   SEQUENCE   96 AA;  11126 MW;  C3D16DA57EF6F588 CRC64;
     MATARDIIKR PIITERSADL MVDKKYTFEV NPRANKVQIR NAVEEIFGVT VTNVNTMNYK
     GKFKRFGRYS GYTRKRKKAI VELSADSKEL EFFEGV
//

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