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Database: UniProt
Entry: Q18CE9
LinkDB: Q18CE9
Original site: Q18CE9 
ID   RL1_PEPD6               Reviewed;         232 AA.
AC   Q18CE9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-JUN-2014, entry version 60.
DE   RecName: Full=50S ribosomal protein L1;
GN   Name=rplA; OrderedLocusNames=CD630_00620;
OS   Peptoclostridium difficile (strain 630) (Clostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Peptoclostridium.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile
CC       in the ribosome, and is involved in E site tRNA release (By
CC       similarity).
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA
CC       (By similarity).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L1P family.
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DR   EMBL; AM180355; CAJ66877.1; -; Genomic_DNA.
DR   RefSeq; YP_001086526.1; NC_009089.1.
DR   ProteinModelPortal; Q18CE9; -.
DR   SMR; Q18CE9; 3-227.
DR   STRING; 272563.CD0062; -.
DR   EnsemblBacteria; CAJ66877; CAJ66877; CD630_00620.
DR   GeneID; 4916675; -.
DR   KEGG; cdf:CD630_00620; -.
DR   PATRIC; 19438263; VBICloDif38397_0073.
DR   eggNOG; COG0081; -.
DR   HOGENOM; HOG000207015; -.
DR   KO; K02863; -.
DR   OMA; MAGKRTQ; -.
DR   OrthoDB; EOG6FBX2G; -.
DR   BioCyc; CDIF272563:GJFE-117-MONOMER; -.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.190.20; -; 2.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016094; Ribosomal_L1_2-a/b-sand.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   TIGRFAMs; TIGR01169; rplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT   CHAIN         1    232       50S ribosomal protein L1.
FT                                /FTId=PRO_0000307992.
SQ   SEQUENCE   232 AA;  24807 MW;  E70108E13DAB99C8 CRC64;
     MAKKGKRYAG ALQKVDRTKF YDASEALTLV SDIAGAKFDE TVEAHIKLGV DSRHADQQVR
     GAVVLPHGTG KTKRVLVFAK GEKAKEAEQA GADFVGAEEL VQKIQGENWF DFDIVVATPD
     MMGVVGRLGR VLGPKGLMPN PKSGTVTFDV AKAIDEIKAG KVEYRLDKTN IIHVPVGKVS
     FGGEKLTENF TALMDAIIKA KPAAAKGQYL RSITVASSMG PGVKINPART AE
//
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