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Database: UniProt
Entry: A0A0S9R994_9ACTN
LinkDB: A0A0S9R994_9ACTN
Original site: A0A0S9R994_9ACTN 
ID   A0A0S9R994_9ACTN        Unreviewed;       101 AA.
AC   A0A0S9R994;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000256|HAMAP-Rule:MF_00537};
GN   Name=rpsN {ECO:0000256|HAMAP-Rule:MF_00537};
GN   ORFNames=ASF37_08145 {ECO:0000313|EMBL:KQP78516.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP78516.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQP78516.1}.
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DR   EMBL; LMNK01000002; KQP78516.1; -; Genomic_DNA.
DR   RefSeq; WP_055963508.1; NZ_LMNK01000002.1.
DR   AlphaFoldDB; A0A0S9R994; -.
DR   OrthoDB; 9810484at2; -.
DR   Proteomes; UP000051640; Unassembled WGS sequence.
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   PANTHER; PTHR19836; 30S RIBOSOMAL PROTEIN S14; 1.
DR   PANTHER; PTHR19836:SF23; 30S RIBOSOMAL PROTEIN S14; 1.
DR   Pfam; PF00253; Ribosomal_S14; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051640};
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          44..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   101 AA;  11552 MW;  9D84352B954A754E CRC64;
     MAKRSKIVAN ERRKEVVERY RERRDALRAA SRDTSLSMAE RMEASRALAG LPRDSSPSRV
     RNRDQVDGRP RGHLRVAGLS RIRFREGAHR GELPGITKSS W
//
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