ID   RS14Z_CLOBM             Reviewed;          61 AA.
AC   B1KSL2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364};
GN   Name=rpsZ {ECO:0000255|HAMAP-Rule:MF_01364};
GN   Synonyms=rpsN {ECO:0000255|HAMAP-Rule:MF_01364};
GN   OrderedLocusNames=CLK_2911;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles
CC       and may also be responsible for determining the conformation of the 16S
CC       rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01364};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01364};
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 and
CC       S10. {ECO:0000255|HAMAP-Rule:MF_01364}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC       Zinc-binding uS14 subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}.
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DR   EMBL; CP000962; ACA54370.1; -; Genomic_DNA.
DR   RefSeq; WP_003357636.1; NC_010520.1.
DR   AlphaFoldDB; B1KSL2; -.
DR   SMR; B1KSL2; -.
DR   EnsemblBacteria; ACA54370; ACA54370; CLK_2911.
DR   GeneID; 5187723; -.
DR   KEGG; cbl:CLK_2911; -.
DR   HOGENOM; CLU_139869_3_0_9; -.
DR   OMA; RAYTRCN; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.830.10; -; 1.
DR   HAMAP; MF_01364_B; Ribosomal_S14_2_B; 1.
DR   InterPro; IPR001209; Ribosomal_S14.
DR   InterPro; IPR043140; Ribosomal_S14/S29.
DR   InterPro; IPR023053; Ribosomal_S14_Z.
DR   PANTHER; PTHR19836; PTHR19836; 1.
DR   Pfam; PF00253; Ribosomal_S14; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Zinc.
FT   CHAIN           1..61
FT                   /note="30S ribosomal protein S14 type Z"
FT                   /id="PRO_1000143893"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
SQ   SEQUENCE   61 AA;  7125 MW;  1ABB8E42EE4DE3AA CRC64;
     MARKALIEKW NKTPKHSTRA YTRCRICGRP HAVLKKYGIC RICFRELAYK GEIPGCKKAS
     W