RS12_LEPBP
ID RS12_LEPBP Reviewed; 124 AA.
AC B0SSI2; P20820; P63197;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=LEPBI_I1969;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=456481;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11470352; DOI=10.1111/j.1574-6968.2001.tb10747.x;
RA Brenot A., Werts C., Ottone C., Sertour N., Charon N.W., Postic D.,
RA Baranton G., Saint Girons I.;
RT "First evidence for a restriction-modification system in Leptospira sp.";
RL FEMS Microbiol. Lett. 201:139-143(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
RN [3]
RP VARIANT STREPTOMYCIN RESISTANT ARG-88.
RX PubMed=11298286; DOI=10.1046/j.1365-2958.2001.02374.x;
RA Picardeau M., Brenot A., Saint Girons I.;
RT "First evidence for gene replacement in Leptospira spp. Inactivation of L.
RT biflexa flaB results in non-motile mutants deficient in endoflagella.";
RL Mol. Microbiol. 40:189-199(2001).
CC -!- FUNCTION: With S4 and S5 plays an important role in translational
CC accuracy. {ECO:0000250}.
CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are
CC involved in tRNA selection in the A site and with the mRNA backbone.
CC Located at the interface of the 30S and 50S subunits, it traverses the
CC body of the 30S subunit contacting proteins on the other side and
CC probably holding the rRNA structure together. The combined cluster of
CC proteins S8, S12 and S17 appears to hold together the shoulder and
CC platform of the 30S subunit (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC S17. May interact with IF1 in the 30S initiation complex (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to the
CC resistant allele in L.biflexa.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; AJ310919; CAC44030.1; -; Genomic_DNA.
DR EMBL; CP000786; ABZ98072.1; -; Genomic_DNA.
DR RefSeq; WP_004783543.1; NC_010602.1.
DR AlphaFoldDB; B0SSI2; -.
DR SMR; B0SSI2; -.
DR STRING; 456481.LEPBI_I1969; -.
DR GeneID; 50044006; -.
DR GeneID; 64279442; -.
DR KEGG; lbi:LEPBI_I1969; -.
DR HOGENOM; CLU_104295_1_2_12; -.
DR OMA; SPALEKC; -.
DR OrthoDB; 1707228at2; -.
DR BioCyc; LBIF456481:LEPBI_RS09730-MON; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd03368; Ribosomal_S12; 1.
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 Antibiotic resistance; Methylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146245"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
FT VARIANT 88
FT /note="K -> R (streptomycin resistant)"
FT /evidence="ECO:0000269|PubMed:11298286"
SQ SEQUENCE 124 AA; 13948 MW; F922286E5CC077C1 CRC64;
MPTINQLIRI GREDQKKRTK SPALKACPQR RGVCTRVMTF TPKKPNSALR KVARVRLTTG
IEVTAYIPGE GHNLQEHNVV LIRGGRVKDL PGVRYHIIRG TLDTLGVDKR RKGRSKYGAK
RPKA
