RS4_MYCS2
ID RS4_MYCS2 Reviewed; 201 AA.
AC A0QSL7; I7F8S3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306};
GN OrderedLocusNames=MSMEG_1523, MSMEI_1487;
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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
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DR EMBL; CP000480; ABK70484.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37960.1; -; Genomic_DNA.
DR RefSeq; WP_003892911.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885905.1; NC_008596.1.
DR PDB; 5O5J; EM; 3.45 A; D=1-201.
DR PDB; 5O61; EM; 3.31 A; BD=1-201.
DR PDB; 5XYU; EM; 3.45 A; D=1-201.
DR PDB; 5ZEB; EM; 3.40 A; d=1-201.
DR PDB; 5ZEP; EM; 3.40 A; d=1-201.
DR PDB; 5ZEU; EM; 3.70 A; d=1-201.
DR PDB; 6DZI; EM; 3.46 A; l=2-201.
DR PDB; 6DZK; EM; 3.60 A; D=1-201.
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; A0QSL7; -.
DR SMR; A0QSL7; -.
DR IntAct; A0QSL7; 2.
DR STRING; 246196.MSMEI_1487; -.
DR PRIDE; A0QSL7; -.
DR EnsemblBacteria; ABK70484; ABK70484; MSMEG_1523.
DR EnsemblBacteria; AFP37960; AFP37960; MSMEI_1487.
DR GeneID; 66732980; -.
DR KEGG; msg:MSMEI_1487; -.
DR KEGG; msm:MSMEG_1523; -.
DR PATRIC; fig|246196.19.peg.1508; -.
DR eggNOG; COG0522; Bacteria.
DR OMA; NVVFRMG; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..201
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000322311"
FT DOMAIN 91..157
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:5O5J"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5O5J"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:5O5J"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5O5J"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:5XYU"
SQ SEQUENCE 201 AA; 23376 MW; F6AC4F66558E0968 CRC64;
MARYTGPATR KSRRLGVDLV GGDQSFEKRP YPPGQHGRAR IKESEYRQQL QEKQKARFSY
GVMEKQFRRY YEEANRQPGK TGDNLLRILE SRLDNVVYRA GLARTRRMAR QLVSHGHFLV
NGVKVDIPSY RVSQYDIIDV KEKSLNTLPF QIARETAGER PIPSWLQVVG ERQRILVHQL
PERAQIDVPL TEQLIVELYS K
