ID A2BMD3_HYPBU Unreviewed; 57 AA.
AC A2BMD3;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000256|HAMAP-Rule:MF_01364};
GN Name=rps14 {ECO:0000256|HAMAP-Rule:MF_01364};
GN OrderedLocusNames=Hbut_1314 {ECO:0000313|EMBL:ABM81144.1};
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM81144.1, ECO:0000313|Proteomes:UP000002593};
RN [1] {ECO:0000313|EMBL:ABM81144.1, ECO:0000313|Proteomes:UP000002593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC {ECO:0000313|Proteomes:UP000002593};
RX PubMed=17350933;
RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles.
CC {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. {ECO:0000256|HAMAP-
CC Rule:MF_01364}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC Zinc-binding uS14 subfamily. {ECO:0000256|HAMAP-Rule:MF_01364}.
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DR EMBL; CP000493; ABM81144.1; -; Genomic_DNA.
DR AlphaFoldDB; A2BMD3; -.
DR STRING; 415426.Hbut_1314; -.
DR EnsemblBacteria; ABM81144; ABM81144; Hbut_1314.
DR KEGG; hbu:Hbut_1314; -.
DR eggNOG; arCOG00782; Archaea.
DR HOGENOM; CLU_177289_2_2_2; -.
DR Proteomes; UP000002593; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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_A; Ribosomal_S14_2_A; 1.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR023676; Ribosomal_uS14_arc.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
DR InterPro; IPR039744; RIbosomal_uS14_euk_arc.
DR InterPro; IPR043140; Ribosomal_uS14_sf.
DR PANTHER; PTHR12010; 40S RIBOSOMAL PROTEIN S29; 1.
DR PANTHER; PTHR12010:SF2; 40S RIBOSOMAL PROTEIN S29; 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:UP000002593};
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|HAMAP-Rule:MF_01364}.
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="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 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 57 AA; 6710 MW; 633EA31E2637AF8C CRC64;
MDDMGKYRPP RVVKYGRGAY RCQRCGSHDA VIKKYGLMLC RQCFRELAVS LGFRKYM
//