ID   RS12_BARHE              Reviewed;         123 AA.
AC   Q8KNX8;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=30S ribosomal protein S12;
GN   Name=rpsL; OrderedLocusNames=BH10560;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=12421311; DOI=10.1046/j.1365-2958.2002.03208.x;
RA   Schulein R., Dehio C.;
RT   "The VirB/VirD4 type IV secretion system of Bartonella is essential for
RT   establishing intraerythrocytic infection.";
RL   Mol. Microbiol. 46:1053-1067(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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 B.henselae.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ315958; CAC51476.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27847.1; -; Genomic_DNA.
DR   RefSeq; WP_011180917.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q8KNX8; -.
DR   SMR; Q8KNX8; -.
DR   STRING; 283166.BH10560; -.
DR   PaxDb; Q8KNX8; -.
DR   PRIDE; Q8KNX8; -.
DR   EnsemblBacteria; CAF27847; CAF27847; BH10560.
DR   GeneID; 64157266; -.
DR   KEGG; bhe:BH10560; -.
DR   eggNOG; COG0048; Bacteria.
DR   OMA; SPALEKC; -.
DR   Proteomes; UP000000421; Chromosome.
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; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..123
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146180"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   123 AA;  13957 MW;  235D72BC638ECE5C CRC64;
     MPTVNQLIRK PRITPIKRNK VPALQSNPQK RGVCTRVYTT TPKKPNSALR KVAKVRLTNG
     FEVIGYIPGE GHNLQEHSVV MIRGGRVKDL PGVRYHIIRG LLDTQGVKNR KQRRSKYGAK
     RPK