ID T2KHF2_FORAG Unreviewed; 89 AA.
AC T2KHF2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BN863_5750 {ECO:0000313|EMBL:CDF78287.1};
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF78287.1, ECO:0000313|Proteomes:UP000016160};
RN [1] {ECO:0000313|EMBL:CDF78287.1, ECO:0000313|Proteomes:UP000016160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901
RC {ECO:0000313|Proteomes:UP000016160};
RX PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
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_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|HAMAP-Rule:MF_00537}.
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DR EMBL; HG315671; CDF78287.1; -; Genomic_DNA.
DR RefSeq; WP_038527313.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KHF2; -.
DR STRING; 1347342.BN863_5750; -.
DR PATRIC; fig|1347342.6.peg.579; -.
DR eggNOG; COG0199; Bacteria.
DR HOGENOM; CLU_139869_0_0_10; -.
DR OrthoDB; 9810484at2; -.
DR Proteomes; UP000016160; Chromosome.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000016160};
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 89 AA; 10140 MW; 845A6990D03D6166 CRC64;
MAKESMKARE VKRAKTVAKY AEKRKALKEA GDYEALQKLP KNASPVRMHN RCKLTGRPKG
YMRTFGISRV TFREMANNGL IPGVRKASW
//
