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RS3_PROA2
ID   RS3_PROA2               Reviewed;         251 AA.
AC   B4S5C2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=Paes_2058;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-
CC       Rule:MF_01309}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01309}.
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DR   EMBL; CP001108; ACF47068.1; -; Genomic_DNA.
DR   RefSeq; WP_012506600.1; NC_011059.1.
DR   AlphaFoldDB; B4S5C2; -.
DR   SMR; B4S5C2; -.
DR   STRING; 290512.Paes_2058; -.
DR   EnsemblBacteria; ACF47068; ACF47068; Paes_2058.
DR   KEGG; paa:Paes_2058; -.
DR   eggNOG; COG0092; Bacteria.
DR   HOGENOM; CLU_058591_0_2_10; -.
DR   OMA; KTNPIGN; -.
DR   OrthoDB; 1132353at2; -.
DR   Proteomes; UP000002725; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1140.32; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
DR   TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..251
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_1000141003"
FT   DOMAIN          39..109
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT   REGION          222..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  28693 MW;  01B188308D57DC42 CRC64;
     MGQKVNPTGF RLGIIRDWTS RWYDDSPVIA EKLKQDHVIR NYVQARLKRE RAGIAKIVIE
     RTTKHIKINI FAARPGAVVG RKGEEINNLS QELSRITGRE VKIDVIEVIK PEIEAQLIGE
     NIAYQLENRV SFRRAMKQAI QQAMRAGAEG IRIRCAGRLG GVEIARSEQY KEGKIPLHTL
     RANVDYASVT AHTIAGAIGI KVWVYKGEVL VQRIDAIEED ELKKIKDRRG EQRSRGRDSR
     NRRRRKPRQT T
 
 
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