ID A9KD18_COXBN Unreviewed; 99 AA.
AC A9KD18;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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:ABS77642.1};
GN OrderedLocusNames=CBUD_1841 {ECO:0000313|EMBL:ABS77642.1};
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922 {ECO:0000313|EMBL:ABS77642.1, ECO:0000313|Proteomes:UP000008555};
RN [1] {ECO:0000313|EMBL:ABS77642.1, ECO:0000313|Proteomes:UP000008555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111 {ECO:0000313|EMBL:ABS77642.1,
RC ECO:0000313|Proteomes:UP000008555};
RX PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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}.
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DR EMBL; CP000733; ABS77642.1; -; Genomic_DNA.
DR RefSeq; WP_005771520.1; NC_009727.1.
DR AlphaFoldDB; A9KD18; -.
DR KEGG; cbd:CBUD_1841; -.
DR HOGENOM; CLU_139869_0_1_6; -.
DR Proteomes; UP000008555; 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 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}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 99 AA; 11568 MW; BD60CE21B9FD64B6 CRC64;
MAKLSVIERN KKRVRKSQSA RKKRLELKKI IKKGTPEEQE QALLKLQKRP RDESPVRTRD
RCRLCGRPCG TFKKFGLCRI HLREAAMRAD VPGLKKASW
//
