RS3_MYCS2
ID RS3_MYCS2 Reviewed; 275 AA.
AC A0QSD7; I7G5M8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309};
GN OrderedLocusNames=MSMEG_1442, MSMEI_1406;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK75343.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37879.1; -; Genomic_DNA.
DR RefSeq; WP_003892829.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885825.1; NC_008596.1.
DR PDB; 5O5J; EM; 3.45 A; C=1-275.
DR PDB; 5O61; EM; 3.31 A; BC=1-275.
DR PDB; 5XYU; EM; 3.45 A; C=1-275.
DR PDB; 5ZEB; EM; 3.40 A; c=1-275.
DR PDB; 5ZEP; EM; 3.40 A; c=1-275.
DR PDB; 5ZEU; EM; 3.70 A; c=1-275.
DR PDB; 6DZI; EM; 3.46 A; k=2-209.
DR PDB; 6DZK; EM; 3.60 A; C=1-275.
DR PDBsum; 5O5J; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5XYU; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZEU; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZK; -.
DR AlphaFoldDB; A0QSD7; -.
DR SMR; A0QSD7; -.
DR IntAct; A0QSD7; 2.
DR STRING; 246196.MSMEI_1406; -.
DR PRIDE; A0QSD7; -.
DR EnsemblBacteria; ABK75343; ABK75343; MSMEG_1442.
DR EnsemblBacteria; AFP37879; AFP37879; MSMEI_1406.
DR GeneID; 66732901; -.
DR KEGG; msg:MSMEI_1406; -.
DR KEGG; msm:MSMEG_1442; -.
DR PATRIC; fig|246196.19.peg.1428; -.
DR eggNOG; COG0092; Bacteria.
DR OMA; KTNPIGN; -.
DR OrthoDB; 1132353at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..275
FT /note="30S ribosomal protein S3"
FT /id="PRO_0000293829"
FT DOMAIN 38..106
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT REGION 215..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:5XYU"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:5O5J"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:5XYU"
SQ SEQUENCE 275 AA; 30139 MW; A76FA94ECBB443BE CRC64;
MGQKINPHGF RLGITTEWKS RWYADKQYKD YVKEDVAIRK LLATGLERAG IADVEIERTR
DRVRVDIHTA RPGIVIGRRG TEADRIRADL EKLTGKQVQL NILEVKNPES QAQLVAQGVA
EQLSNRVAFR RAMRKAIQSA MRQPNVKGIR VQCSGRLGGA EMSRSEFYRE GRVPLHTLRA
DIDYGLYEAK TTFGRIGVKV WIYKGDIVGG KRELAAAAPA SDRPRRERPS GTRPRRSGSA
GTTATSTEAG RAATSDAPAA GTAAAAEAPA ESTES
