ID A0A2K4C083_9STAP Unreviewed; 61 AA.
AC A0A2K4C083;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000256|HAMAP-Rule:MF_01364};
GN Name=rpsZ {ECO:0000256|HAMAP-Rule:MF_01364};
GN Synonyms=rpsN {ECO:0000256|HAMAP-Rule:MF_01364};
GN ORFNames=CD158_04240 {ECO:0000313|EMBL:PNZ67982.1};
OS Staphylococcus auricularis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=29379 {ECO:0000313|EMBL:PNZ67982.1, ECO:0000313|Proteomes:UP000242470};
RN [1] {ECO:0000313|EMBL:PNZ67982.1, ECO:0000313|Proteomes:UP000242470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12101 {ECO:0000313|EMBL:PNZ67982.1,
RC ECO:0000313|Proteomes:UP000242470};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01364}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01364};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01364};
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 and
CC S10. {ECO:0000256|HAMAP-Rule:MF_01364}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC Zinc-binding uS14 subfamily. {ECO:0000256|HAMAP-Rule:MF_01364}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNZ67982.1}.
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DR EMBL; PPQW01000021; PNZ67982.1; -; Genomic_DNA.
DR RefSeq; WP_059107576.1; NZ_VTQJ01000006.1.
DR STRING; 29379.GCA_001500315_00407; -.
DR GeneID; 64981581; -.
DR KEGG; saul:I6G39_02955; -.
DR OrthoDB; 9810484at2; -.
DR Proteomes; UP000242470; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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 HAMAP; MF_01364_B; Ribosomal_S14_2_B; 1.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR023053; Ribosomal_uS14_bact.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
DR InterPro; IPR043140; Ribosomal_uS14_sf.
DR PANTHER; PTHR19836; 30S RIBOSOMAL PROTEIN S14; 1.
DR PANTHER; PTHR19836:SF26; 30S RIBOSOMAL PROTEIN S14 TYPE Z; 1.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01364};
KW Reference proteome {ECO:0000313|Proteomes:UP000242470};
KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01364};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01364,
KW ECO:0000313|EMBL:PNZ67982.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01364};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01364};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01364}.
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
SQ SEQUENCE 61 AA; 7313 MW; EDE46D762F839822 CRC64;
MAKSSMVAKQ QQNKKFKVRE YTRCERCGRP HSVYRKFKLC RICFRELAYK GQIPGVRKAS
W
//