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Database: UniProt
Entry: A5I7J5
LinkDB: A5I7J5
Original site: A5I7J5 
ID   RL24_CLOBH              Reviewed;         105 AA.
AC   A5I7J5; A7G8S7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   19-FEB-2014, entry version 54.
DE   RecName: Full=50S ribosomal protein L24;
GN   Name=rplX; OrderedLocusNames=CBO3470, CLC_3414;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
RA   Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
RA   Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
RA   Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
RA   Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum
RT   strain Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-
RT   A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds
CC       directly to the 5'-end of the 23S rRNA, where it nucleates
CC       assembly of the 50S subunit (By similarity).
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit (By similarity).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L24P family.
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DR   EMBL; CP000727; ABS36236.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL85030.1; -; Genomic_DNA.
DR   RefSeq; YP_001255951.1; NC_009495.1.
DR   RefSeq; YP_001389192.1; NC_009698.1.
DR   ProteinModelPortal; A5I7J5; -.
DR   STRING; 413999.CBO3470; -.
DR   EnsemblBacteria; ABS36236; ABS36236; CLC_3414.
DR   GeneID; 5187724; -.
DR   GeneID; 5398659; -.
DR   KEGG; cbh:CLC_3414; -.
DR   KEGG; cbo:CBO3470; -.
DR   PATRIC; 19369069; VBICloBot22612_3446.
DR   eggNOG; COG0198; -.
DR   HOGENOM; HOG000039891; -.
DR   KO; K02895; -.
DR   OMA; DIEAPIH; -.
DR   OrthoDB; EOG6FFSDM; -.
DR   ProtClustDB; PRK00004; -.
DR   BioCyc; CBOT413999:GJ72-3603-MONOMER; -.
DR   BioCyc; CBOT441771:GIWX-3361-MONOMER; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR003256; Ribosomal_L24.
DR   InterPro; IPR008991; Translation_prot_SH3-like.
DR   PANTHER; PTHR12903; PTHR12903; 1.
DR   Pfam; PF00467; KOW; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01079; rplX_bact; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1    105       50S ribosomal protein L24.
FT                                /FTId=PRO_0000355660.
SQ   SEQUENCE   105 AA;  11709 MW;  9FECA8BC2D52989F CRC64;
     MSKIHVRKKD TVVVISGKDK SKIGEVLSVL PKKGKVIVKD VNVVTKHQKP NRENMQGGII
     HKEAPIFSSK VMLYCDKCKS ATRISNKILE DGTKVRVCKK CGETF
//
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