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Database: UniProt
Entry: A0A240UFN1_9BURK
LinkDB: A0A240UFN1_9BURK
Original site: A0A240UFN1_9BURK 
ID   A0A240UFN1_9BURK        Unreviewed;        93 AA.
AC   A0A240UFN1; A0A240TV58; A0A240U5A1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Small ribosomal subunit protein bS18 {ECO:0000256|HAMAP-Rule:MF_00270};
GN   Name=rpsR {ECO:0000256|HAMAP-Rule:MF_00270};
GN   ORFNames=CBP33_13630 {ECO:0000313|EMBL:ART49037.1}, CBP34_14160
GN   {ECO:0000313|EMBL:ART52573.1}, CBP36_14175
GN   {ECO:0000313|EMBL:ART59820.1};
OS   Acidovorax carolinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=553814 {ECO:0000313|EMBL:ART59820.1, ECO:0000313|Proteomes:UP000194440};
RN   [1] {ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA2 {ECO:0000313|EMBL:ART49037.1}, NA3
RC   {ECO:0000313|EMBL:ART52573.1}, and P4 {ECO:0000313|EMBL:ART59820.1};
RA   Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA   Aitken M.D.;
RT   "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT   Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds as a heterodimer with protein bS6 to the central domain
CC       of the 16S rRNA, where it helps stabilize the platform of the 30S
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_00270}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight heterodimer
CC       with protein bS6. {ECO:0000256|HAMAP-Rule:MF_00270}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.
CC       {ECO:0000256|ARBA:ARBA00005589, ECO:0000256|HAMAP-Rule:MF_00270,
CC       ECO:0000256|RuleBase:RU003910}.
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DR   EMBL; CP021359; ART49037.1; -; Genomic_DNA.
DR   EMBL; CP021361; ART52573.1; -; Genomic_DNA.
DR   EMBL; CP021366; ART59820.1; -; Genomic_DNA.
DR   RefSeq; WP_005795932.1; NZ_CP021366.1.
DR   AlphaFoldDB; A0A240UFN1; -.
DR   SMR; A0A240UFN1; -.
DR   GeneID; 77322307; -.
DR   KEGG; acid:CBP33_13630; -.
DR   KEGG; acin:CBP34_14160; -.
DR   KEGG; acip:CBP36_14175; -.
DR   OrthoDB; 9812008at2; -.
DR   Proteomes; UP000194432; Chromosome.
DR   Proteomes; UP000194440; Chromosome.
DR   Proteomes; UP000194504; Chromosome.
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; 4.10.640.10; Ribosomal protein S18; 1.
DR   HAMAP; MF_00270; Ribosomal_S18; 1.
DR   InterPro; IPR001648; Ribosomal_bS18.
DR   InterPro; IPR036870; Ribosomal_bS18_sf.
DR   NCBIfam; TIGR00165; S18; 1.
DR   PANTHER; PTHR13479:SF40; 28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13479; 30S RIBOSOMAL PROTEIN S18; 1.
DR   Pfam; PF01084; Ribosomal_S18; 1.
DR   PRINTS; PR00974; RIBOSOMALS18.
DR   SUPFAM; SSF46911; Ribosomal protein S18; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194432};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00270};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00270}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00270};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00270}.
SQ   SEQUENCE   93 AA;  10992 MW;  0EDD1AF32B1B9F34 CRC64;
     MATFKKFNKD KRPKRNTQSL LFKRKRFCRF TVTGVEEIDY KDVDTLRDFI AENGKIIPAR
     LTGTRAIFQR QLNTAIKRAR FLALVPYSDQ HKI
//
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