GenomeNet

Database: UniProt
Entry: A0QL38
LinkDB: A0QL38
Original site: A0QL38 
ID   RS12_MYCA1              Reviewed;         124 AA.
AC   A0QL38;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   19-FEB-2014, entry version 49.
DE   RecName: Full=30S ribosomal protein S12;
GN   Name=rpsL; OrderedLocusNames=MAV_4492;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy (By similarity).
CC   -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
CC       are involved in tRNA selection in the A site and with the mRNA
CC       backbone. Located at the interface of the 30S and 50S subunits, it
CC       traverses the body of the 30S subunit contacting proteins on the
CC       other side and probably holding the rRNA structure together. The
CC       combined cluster of proteins S8, S12 and S17 appears to hold
CC       together the shoulder and platform of the 30S subunit (By
CC       similarity).
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8
CC       and S17. May interact with IF1 in the 30S initiation complex (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S12P family.
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DR   EMBL; CP000479; ABK68750.1; -; Genomic_DNA.
DR   RefSeq; YP_883626.1; NC_008595.1.
DR   ProteinModelPortal; A0QL38; -.
DR   SMR; A0QL38; 1-123.
DR   STRING; 243243.MAV_4492; -.
DR   EnsemblBacteria; ABK68750; ABK68750; MAV_4492.
DR   GeneID; 4529115; -.
DR   KEGG; mav:MAV_4492; -.
DR   PATRIC; 17990679; VBIMycAvi38287_4413.
DR   eggNOG; COG0048; -.
DR   HOGENOM; HOG000040063; -.
DR   KO; K02950; -.
DR   OMA; GTMTPRK; -.
DR   OrthoDB; EOG61ZTNF; -.
DR   ProtClustDB; PRK05163; -.
DR   BioCyc; MAVI243243:GH3Y-4492-MONOMER; -.
DR   GO; GO:0015935; C:small 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-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005679; Ribosomal_S12_bac.
DR   PANTHER; PTHR11652; PTHR11652; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00981; rpsL_bact; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN         1    124       30S ribosomal protein S12.
FT                                /FTId=PRO_0000295999.
FT   MOD_RES      89     89       3-methylthioaspartic acid (By
FT                                similarity).
SQ   SEQUENCE   124 AA;  13849 MW;  2B29ADD44DFB7188 CRC64;
     MPTIQQLVRK GRRDKIGKVK TAALKGSPQR RGVCTRVYTT TPKKPNSALR KVARVKLTSQ
     VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
     KEKS
//
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