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Database: UniProt
Entry: Q2GFN3
LinkDB: Q2GFN3
Original site: Q2GFN3 
ID   RS12_EHRCR              Reviewed;         123 AA.
AC   Q2GFN3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Small ribosomal subunit protein uS12 {ECO:0000255|HAMAP-Rule:MF_00403};
DE   AltName: Full=30S ribosomal protein S12 {ECO:0000305};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=ECH_0963;
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}.
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. {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC       S17. May interact with IF1 in the 30S initiation complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00403}.
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DR   EMBL; CP000236; ABD44798.1; -; Genomic_DNA.
DR   RefSeq; WP_006010363.1; NC_007799.1.
DR   AlphaFoldDB; Q2GFN3; -.
DR   SMR; Q2GFN3; -.
DR   STRING; 205920.ECH_0963; -.
DR   KEGG; ech:ECH_0963; -.
DR   eggNOG; COG0048; Bacteria.
DR   HOGENOM; CLU_104295_1_2_5; -.
DR   OrthoDB; 9802366at2; -.
DR   Proteomes; UP000008320; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd03368; Ribosomal_S12; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00403_B; Ribosomal_uS12_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_uS12.
DR   InterPro; IPR005679; Ribosomal_uS12_bac.
DR   NCBIfam; TIGR00981; rpsL_bact; 1.
DR   PANTHER; PTHR11652:SF1; 28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11652; 30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   3: Inferred from homology;
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..123
FT                   /note="Small ribosomal subunit protein uS12"
FT                   /id="PRO_0000295973"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         90
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   123 AA;  13688 MW;  5E0864A3065BA022 CRC64;
     MPTINQLVRK PRKSRSSLNK APALQHNPQK RAVCVKVYTT TPKKPNSALR KVARVKIAGY
     GSEVIAYIPG EGHNLQEHSV ILIRGGRVKD LPGVRYHIIR GALDSRGVQN RKKARSKYGV
     KKS
//
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