ID A8V0R0_9AQUI Unreviewed; 62 AA.
AC A8V0R0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000256|ARBA:ARBA00035167, 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=HG1285_03889 {ECO:0000313|EMBL:EDP73987.1};
OS Hydrogenivirga sp. 128-5-R1-1.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP73987.1, ECO:0000313|Proteomes:UP000005981};
RN [1] {ECO:0000313|EMBL:EDP73987.1, ECO:0000313|Proteomes:UP000005981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP73987.1,
RC ECO:0000313|Proteomes:UP000005981};
RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP73987.1}.
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DR EMBL; ABHJ01000100; EDP73987.1; -; Genomic_DNA.
DR AlphaFoldDB; A8V0R0; -.
DR PATRIC; fig|392423.7.peg.1136; -.
DR OrthoDB; 9810484at2; -.
DR Proteomes; UP000005981; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF19; 28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19836; 30S RIBOSOMAL PROTEIN S14; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01364}; Reference proteome {ECO:0000313|Proteomes:UP000005981};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01364};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01364}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01364};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01364};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01364}.
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01364"
SQ SEQUENCE 62 AA; 7386 MW; C3C811B4F3410723 CRC64;
MARKALWAKS FLKEPKFKTR KHSRCPLCGR PRGYIRQFDM CRICFRERAS RGEIPGIKKA
SW
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