(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHR7_GEOS0

ID   A0A0F6BHR7_GEOS0        Unreviewed;        95 AA.
AC   A0A0F6BHR7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 23.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000256|HAMAP-Rule:MF_01369, ECO:0000256|RuleBase:RU003935};
GN   Name=rplW {ECO:0000256|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=GY4MC1_0112 {ECO:0000313|EMBL:ADP72968.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72968.1};
RN   [1] {ECO:0000313|EMBL:ADP72968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72968.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC       the proteins that surrounds the polypeptide exit tunnel on the outside
CC       of the ribosome. Forms the main docking site for trigger factor binding
CC       to the ribosome. {ECO:0000256|HAMAP-Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC       trigger factor when it is bound to the ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01369, ECO:0000256|RuleBase:RU003934}.
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DR   EMBL; CP002293; ADP72968.1; -; Genomic_DNA.
DR   RefSeq; WP_003247564.1; NC_014650.1.
DR   EnsemblBacteria; ADP72968; ADP72968; GY4MC1_0112.
DR   GeneID; 29237252; -.
DR   KEGG; gmc:GY4MC1_0112; -.
DR   KO; K02892; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
DR   BioCyc; GSP581103:G1GOQ-139-MONOMER; -.
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; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHR7.
DR   SWISS-2DPAGE; A0A0F6BHR7.
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01369,
KW   ECO:0000256|RuleBase:RU003934};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01369,
KW   ECO:0000256|RuleBase:RU003934, ECO:0000313|EMBL:ADP72968.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01369,
KW   ECO:0000256|RuleBase:RU003935};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01369,
KW   ECO:0000256|RuleBase:RU003935}.
SQ   SEQUENCE   95 AA;  11069 MW;  FF32C6DBD34FEA7A CRC64;
     MKDPRDIIKR PIITENTMNL ISQKKYTFEV DVNANKTEVK DAVEKIFGVK VAKVNIMNYK
     GKFKRVGRYS GYTNRRRKAI VTLTPDSKEI ELFEV
//

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