ID   RS14Z_LEPBA             Reviewed;          61 AA.
AC   B0SA34;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=LBF_1900;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / Ames;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000777; ABZ94404.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0SA34; -.
DR   SMR; B0SA34; -.
DR   KEGG; lbf:LBF_1900; -.
DR   HOGENOM; CLU_139869_3_0_12; -.
DR   OMA; RAYTRCN; -.
DR   BioCyc; LBIF355278:LBF_RS18905-MON; -.
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_1000143912"
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;  7329 MW;  0AFFE2139A03D25F CRC64;
     MAKKSMMERH AKEQKFKVRE YNRCPLCGRS RAYLRRFDMC RLCFRDLASK AQIPGVKKSS
     W