ID   IOJAP_ZYMMO             Reviewed;         133 AA.
AC   Q5NLX3;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ribosomal silencing factor RsfS {ECO:0000255|HAMAP-Rule:MF_01477};
GN   Name=rsfS {ECO:0000255|HAMAP-Rule:MF_01477}; OrderedLocusNames=ZMO1663;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RA   Chang C., Li H., Bearden J., Joachimiak A.;
RT   "Crystal structure of Iojap-like protein from Zymomonas mobilis.";
RL   Submitted (NOV-2011) to the PDB data bank.
CC   -!- FUNCTION: Functions as a ribosomal silencing factor. Interacts with
CC       ribosomal protein L14 (rplN), blocking formation of intersubunit bridge
CC       B8. Prevents association of the 30S and 50S ribosomal subunits and the
CC       formation of functional ribosomes, thus repressing translation.
CC       {ECO:0000255|HAMAP-Rule:MF_01477}.
CC   -!- SUBUNIT: Interacts with ribosomal protein L14 (rplN).
CC       {ECO:0000255|HAMAP-Rule:MF_01477}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01477}.
CC   -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000255|HAMAP-
CC       Rule:MF_01477}.
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DR   EMBL; AE008692; AAV90287.1; -; Genomic_DNA.
DR   RefSeq; WP_011241412.1; NZ_CP035711.1.
DR   PDB; 3UPS; X-ray; 1.75 A; A=1-133.
DR   PDBsum; 3UPS; -.
DR   AlphaFoldDB; Q5NLX3; -.
DR   SMR; Q5NLX3; -.
DR   STRING; 264203.ZMO1663; -.
DR   EnsemblBacteria; AAV90287; AAV90287; ZMO1663.
DR   GeneID; 58027378; -.
DR   KEGG; zmo:ZMO1663; -.
DR   eggNOG; COG0799; Bacteria.
DR   HOGENOM; CLU_092688_6_0_5; -.
DR   OMA; VVHVFQK; -.
DR   OrthoDB; 1990650at2; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0090071; P:negative regulation of ribosome biogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-UniRule.
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..133
FT                   /note="Ribosomal silencing factor RsfS"
FT                   /id="PRO_0000419628"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   HELIX           58..76
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   HELIX           105..116
FT                   /evidence="ECO:0007829|PDB:3UPS"
FT   TURN            117..120
FT                   /evidence="ECO:0007829|PDB:3UPS"
SQ   SEQUENCE   133 AA;  14543 MW;  0FB3D4229B64654F CRC64;
     MPAPSSPRKN QTSFDPEMLL KLVTDSLDDD QALEIATIPL AGKSSIADYM VIASGRSSRQ
     VTAMAQKLAD RIKAATGYVS KIEGLPAADW VLLDAGDIII HLFRPEVRSF YNLERMWGFG
     DESDQPVSQS VLS