ID C3LRP5_VIBCM Unreviewed; 101 AA.
AC C3LRP5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 ECO:0000313|EMBL:ACP06800.1};
GN OrderedLocusNames=VCM66_2503 {ECO:0000313|EMBL:ACP06800.1};
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP06800.1, ECO:0000313|Proteomes:UP000001217};
RN [1] {ECO:0000313|EMBL:ACP06800.1, ECO:0000313|Proteomes:UP000001217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2 {ECO:0000313|EMBL:ACP06800.1,
RC ECO:0000313|Proteomes:UP000001217};
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001233; ACP06800.1; -; Genomic_DNA.
DR RefSeq; WP_001118926.1; NC_012578.1.
DR AlphaFoldDB; C3LRP5; -.
DR SMR; C3LRP5; -.
DR GeneID; 69718813; -.
DR KEGG; vcm:VCM66_2503; -.
DR HOGENOM; CLU_139869_0_1_6; -.
DR Proteomes; UP000001217; Chromosome I.
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 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; 11610 MW; 81E94F223CF768EA CRC64;
MAKQSMKARE EKRAKLVAQF AEKRATLKAI ISDVNASEED RWNAVLKLQS LPRDSSRSRQ
RNRCNQTGRP HGFLRKFGLS RIKVREACMK GEIPGLRKAS W
//
