ID   RS14Z_CAMJR             Reviewed;          61 AA.
AC   Q5HSA3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; OrderedLocusNames=CJE1862;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW36284.1; -; Genomic_DNA.
DR   RefSeq; WP_002851478.1; NC_003912.7.
DR   AlphaFoldDB; Q5HSA3; -.
DR   SMR; Q5HSA3; -.
DR   KEGG; cjr:CJE1862; -.
DR   HOGENOM; CLU_139869_3_0_7; -.
DR   OMA; RAYTRCN; -.
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; IPR018271; Ribosomal_S14_CS.
DR   InterPro; IPR023053; Ribosomal_S14_Z.
DR   PANTHER; PTHR19836; PTHR19836; 1.
DR   Pfam; PF00253; Ribosomal_S14; 1.
DR   PROSITE; PS00527; 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_0000269088"
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;  6956 MW;  1E4D6A226B4FA002 CRC64;
     MAKKSMIAKA ARKPKFKVRA YTRCQICGRP HSVYRDFGIC RVCLRKMGNE GLIPGLKKAS
     W