ID B8D5V6_DESA1 Unreviewed; 54 AA.
AC B8D5V6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=DKAM_1161 {ECO:0000313|EMBL:ACL11487.1};
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11487.1, ECO:0000313|Proteomes:UP000006903};
RN [1] {ECO:0000313|EMBL:ACL11487.1, ECO:0000313|Proteomes:UP000006903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC {ECO:0000313|Proteomes:UP000006903};
RX PubMed=19114480; DOI=10.1128/JB.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
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; CP001140; ACL11487.1; -; Genomic_DNA.
DR RefSeq; WP_012608828.1; NC_011766.1.
DR AlphaFoldDB; B8D5V6; -.
DR STRING; 490899.DKAM_1161; -.
DR GeneID; 7171248; -.
DR KEGG; dka:DKAM_1161; -.
DR eggNOG; arCOG00782; Archaea.
DR HOGENOM; CLU_177289_2_2_2; -.
DR Proteomes; UP000006903; 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 PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01364};
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 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="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 37
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"
SQ SEQUENCE 54 AA; 6298 MW; BADD6AA368DE4DA5 CRC64;
MAKYKPPKIY KYGRGVQVCR RCGSRDAVIQ AYGLYLCRQC FREVASVIGF KKYE
//
