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Database: UniProt
Entry: Q7VA02
LinkDB: Q7VA02
Original site: Q7VA02 
ID   RS12_PROMA              Reviewed;         124 AA.
AC   Q7VA02;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
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};
GN   Synonyms=rps12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   OrderedLocusNames=Pro_1667;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00711.1; -; Genomic_DNA.
DR   RefSeq; NP_876058.1; NC_005042.1.
DR   RefSeq; WP_011125816.1; NC_005042.1.
DR   AlphaFoldDB; Q7VA02; -.
DR   SMR; Q7VA02; -.
DR   STRING; 167539.Pro_1667; -.
DR   EnsemblBacteria; AAQ00711; AAQ00711; Pro_1667.
DR   KEGG; pma:Pro_1667; -.
DR   PATRIC; fig|167539.5.peg.1761; -.
DR   eggNOG; COG0048; Bacteria.
DR   HOGENOM; CLU_104295_1_2_3; -.
DR   OrthoDB; 9802366at2; -.
DR   Proteomes; UP000001420; 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..124
FT                   /note="Small ribosomal subunit protein uS12"
FT                   /id="PRO_0000146287"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13917 MW;  F8C90EF12497AE79 CRC64;
     MPTIQQLIRT ERQRLTRKTK SPALRSCPER RGVCTRVYTS TPKKPNSALR KVARVRLTSG
     FEVTAYIPGI GHNLQEHSVV LLRGGRVKDL PGVRYHIIRG TLDTAGVKDR RQARSKYGAK
     APKS
//
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