IOJAP_ECOLI
ID IOJAP_ECOLI Reviewed; 105 AA.
AC P0AAT6; P05848; P77107;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ribosomal silencing factor RsfS;
GN Name=rsfS; Synonyms=rsfA, slm3, ybeB; OrderedLocusNames=b0637, JW5090;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3533535; DOI=10.1111/j.1432-1033.1986.tb09961.x;
RA Asoh S., Matsuzawa H., Ishino F., Strominger J.L., Matsuhashi M., Ohta T.;
RT "Nucleotide sequence of the pbpA gene and characteristics of the deduced
RT amino acid sequence of penicillin-binding protein 2 of Escherichia coli
RT K12.";
RL Eur. J. Biochem. 160:231-238(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND ASSOCIATION
RP WITH THE 50S RIBOSOMAL SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16980477; DOI=10.1128/jb.00444-06;
RA Jiang M., Datta K., Walker A., Strahler J., Bagamasbad P., Andrews P.C.,
RA Maddock J.R.;
RT "The Escherichia coli GTPase CgtAE is involved in late steps of large
RT ribosome assembly.";
RL J. Bacteriol. 188:6757-6770(2006).
RN [7]
RP FUNCTION, INTERACTION WITH RIBOSOMAL PROTEIN L14 (RPLN), AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22829778; DOI=10.1371/journal.pgen.1002815;
RA Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F.,
RA Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T.,
RA Diefenbacher M.E., Nierhaus K.H., Uetz P.;
RT "RsfA (YbeB) proteins are conserved ribosomal silencing factors.";
RL PLoS Genet. 8:E1002815-E1002815(2012).
CC -!- FUNCTION: Functions as a ribosomal silencing factor. Addition to
CC isolated ribosomal subunits partially inhibits their association,
CC preventing translation. Interacts with ribosomal protein L14 (rplN),
CC blocking formation of intersubunit bridge B8, preventing association of
CC the 30S and 50S ribosomal subunits and the formation of functional
CC ribosomes, thus repressing translation. {ECO:0000269|PubMed:22829778}.
CC -!- SUBUNIT: Interacts with ribosomal protein L14 (rplN).
CC {ECO:0000269|PubMed:22829778}.
CC -!- INTERACTION:
CC P0AAT6; P33348: yehL; NbExp=3; IntAct=EBI-560192, EBI-489750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16980477}.
CC Note=Comigrates with the 50S ribosomal subunit in sucrose gradients,
CC specifically with ribosomal protein L14 (rplN).
CC -!- DISRUPTION PHENOTYPE: Cell viability is dramatically reduced in
CC stationary phase, cells have a 10 hour growth block upon transition
CC from rich to poor medium. Protein translation in stationary phase is
CC derepressed. {ECO:0000269|PubMed:22829778}.
CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28199.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X04516; CAA28199.1; ALT_INIT; Genomic_DNA.
DR EMBL; U82598; AAB40837.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73738.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35284.2; -; Genomic_DNA.
DR RefSeq; NP_415170.4; NC_000913.3.
DR RefSeq; WP_001161664.1; NZ_STEB01000031.1.
DR PDB; 7BL2; EM; 3.70 A; 6=1-105.
DR PDB; 7BL3; EM; 3.50 A; 6=1-105.
DR PDB; 7BL4; EM; 2.40 A; 6=1-105.
DR PDB; 7BL5; EM; 3.30 A; 6=1-105.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL4; -.
DR PDBsum; 7BL5; -.
DR AlphaFoldDB; P0AAT6; -.
DR SMR; P0AAT6; -.
DR BioGRID; 4261658; 43.
DR DIP; DIP-48141N; -.
DR IntAct; P0AAT6; 10.
DR STRING; 511145.b0637; -.
DR jPOST; P0AAT6; -.
DR PaxDb; P0AAT6; -.
DR PRIDE; P0AAT6; -.
DR EnsemblBacteria; AAC73738; AAC73738; b0637.
DR EnsemblBacteria; BAA35284; BAA35284; BAA35284.
DR GeneID; 66671089; -.
DR GeneID; 945237; -.
DR KEGG; ecj:JW5090; -.
DR KEGG; eco:b0637; -.
DR PATRIC; fig|1411691.4.peg.1631; -.
DR EchoBASE; EB1235; -.
DR eggNOG; COG0799; Bacteria.
DR HOGENOM; CLU_092688_6_1_6; -.
DR InParanoid; P0AAT6; -.
DR OMA; VVHVFQK; -.
DR PhylomeDB; P0AAT6; -.
DR BioCyc; EcoCyc:EG11255-MON; -.
DR PRO; PR:P0AAT6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01477; Iojap_RsfS; 1.
DR InterPro; IPR004394; Iojap/RsfS/C7orf30.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR21043; PTHR21043; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Repressor;
KW Translation regulation.
FT CHAIN 1..105
FT /note="Ribosomal silencing factor RsfS"
FT /id="PRO_0000168674"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:7BL4"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:7BL4"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:7BL4"
SQ SEQUENCE 105 AA; 11582 MW; 7C1315607BD0B610 CRC64;
MQGKALQDFV IDKIDDLKGQ DIIALDVQGK SSITDCMIIC TGTSSRHVMS IADHVVQESR
AAGLLPLGVE GENSADWIVV DLGDVIVHVM QEESRRLYEL EKLWS
