RR4_CHLRE
ID RR4_CHLRE Reviewed; 257 AA.
AC P48270; B7U1G2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=137c / CC-125;
RX PubMed=7770034; DOI=10.1007/bf00293197;
RA Randolph-Anderson B.L., Boynton J.E., Gillham N.W., Huang C., Liu X.-Q.;
RT "The chloroplast gene encoding ribosomal protein S4 in Chlamydomonas
RT reinhardtii spans an inverted repeat -- unique sequence junction and can be
RT mutated to suppress a streptomycin dependence mutation in ribosomal protein
RT S12.";
RL Mol. Gen. Genet. 247:295-305(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP PROTEIN SEQUENCE OF 55-70; 77-84; 112-118 AND 198-215.
RC STRAIN=Arg7/cw15;
RX PubMed=12417713; DOI=10.1105/tpc.004341;
RA Yamaguchi K., Prieto S., Beligni M.V., Haynes P.A., McDonald W.H.,
RA Yates J.R. III, Mayfield S.P.;
RT "Proteomic characterization of the small subunit of Chlamydomonas
RT reinhardtii chloroplast ribosome: identification of a novel S1 domain-
RT containing protein and unusually large orthologs of bacterial S2, S3, and
RT S5.";
RL Plant Cell 14:2957-2974(2002).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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:0000250}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; U17357; AAA81363.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50109.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00921.1; -; Genomic_DNA.
DR PIR; S55251; S55251.
DR RefSeq; NP_958376.1; NC_005353.1.
DR AlphaFoldDB; P48270; -.
DR SMR; P48270; -.
DR STRING; 3055.DAA00921; -.
DR PaxDb; P48270; -.
DR PRIDE; P48270; -.
DR GeneID; 2716955; -.
DR KEGG; cre:ChreCp020; -.
DR eggNOG; KOG3301; Eukaryota.
DR HOGENOM; CLU_092403_0_1_1; -.
DR InParanoid; P48270; -.
DR OrthoDB; 1507367at2759; -.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 2.
DR Gene3D; 3.10.290.10; -; 2.
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; 2.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 2.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 2.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 2.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 2.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..257
FT /note="30S ribosomal protein S4, chloroplastic"
FT /id="PRO_0000132556"
FT DOMAIN 110..170
FT /note="S4 RNA-binding 1"
FT DOMAIN 189..255
FT /note="S4 RNA-binding 2"
FT VARIANT 73
FT /note="Q -> P (in CC-3008; suppresses streptomycin
FT dependence of the S12 mutant P90L)"
FT VARIANT 90
FT /note="V -> GITERQLVNYV (in CC-3010; suppresses
FT streptomycin dependence of the S12 mutant P90L)"
FT VARIANT 92
FT /note="K -> IVNYVRK (in CC-3009; suppresses streptomycin
FT dependence of the S12 mutant P90L)"
SQ SEQUENCE 257 AA; 30018 MW; 006667C4A654E762 CRC64;
MSRYLGPRLR VIRRIGKLRG FTRKKPFRRV FKGFGGFKGK VIPPGQHGLT KLLKTRPYDS
SESDYLIRLK VKQRLRFNYG ITERQLVNYV RKAKKIKEST GQVLLQFLEM RLDNIVFRLN
MAPTIPAARQ LISHGHIRVN NKKVNIPSYM CKPKDVISVA MKQRSLQLVN KNLQEYYRRM
RFYKKRLEKT LPFILLKIKP LGLTSVTAAV ELITKGNVRV NNKSVKTPNY ICRPRDTVSL
RTKQGIKKVF LKNYLKG
