ID Q1YNF5_AURMS Unreviewed; 101 AA.
AC Q1YNF5;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 08-NOV-2023, entry version 60.
DE RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000256|ARBA:ARBA00035167, ECO:0000256|HAMAP-Rule:MF_00537};
GN Name=rpsN {ECO:0000256|HAMAP-Rule:MF_00537};
GN ORFNames=SI859A1_01883 {ECO:0000313|EMBL:EAS51076.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51076.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS51076.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51076.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(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:0000256|ARBA:ARBA00003686, ECO:0000256|HAMAP-
CC Rule:MF_00537}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 and
CC S10. {ECO:0000256|HAMAP-Rule:MF_00537}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000256|ARBA:ARBA00009083, ECO:0000256|HAMAP-Rule:MF_00537}.
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:EAS51076.1}.
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DR EMBL; AAPJ01000001; EAS51076.1; -; Genomic_DNA.
DR RefSeq; WP_009209722.1; NZ_CH672387.1.
DR AlphaFoldDB; Q1YNF5; -.
DR HOGENOM; CLU_139869_0_1_5; -.
DR OrthoDB; 9810484at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_01883-MONOMER; -.
DR Proteomes; UP000000321; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.1480; -; 1.
DR HAMAP; MF_00537; Ribosomal_S14_1; 1.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR023036; Ribosomal_uS14_bac/plastid.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
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 Reference proteome {ECO:0000313|Proteomes:UP000000321};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00537};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00537}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00537};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00537}.
SQ SEQUENCE 101 AA; 11552 MW; FF491D1B15DCD1F8 CRC64;
MAKKGMIEQN KHRQKMVAKY AAKRAALKAI TKNADAPMEE RFQAQLQLAE LPRNGSKVRI
RNRCEVTGRP RAYYRKLKMS RIALRDLGNN GQIPGIVKSS W
//
