ID A0A0F4RL35_9RHOB Unreviewed; 75 AA.
AC A0A0F4RL35;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Small ribosomal subunit protein bS18 {ECO:0000256|ARBA:ARBA00035141, ECO:0000256|HAMAP-Rule:MF_00270};
GN Name=rpsR {ECO:0000256|HAMAP-Rule:MF_00270};
GN ORFNames=TW80_05930 {ECO:0000313|EMBL:KJZ20344.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20344.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ20344.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ20344.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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}.
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:KJZ20344.1}.
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DR EMBL; JXYE01000002; KJZ20344.1; -; Genomic_DNA.
DR RefSeq; WP_045996359.1; NZ_JXYE01000002.1.
DR AlphaFoldDB; A0A0F4RL35; -.
DR STRING; 579483.TW80_05930; -.
DR PATRIC; fig|579483.3.peg.1213; -.
DR OrthoDB; 9812008at2; -.
DR Proteomes; UP000033741; 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; 4.10.640.10; Ribosomal protein S18; 1.
DR HAMAP; MF_00270; Ribosomal_S18; 1.
DR InterPro; IPR001648; Ribosomal_bS18.
DR InterPro; IPR018275; Ribosomal_bS18_CS.
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.
DR PROSITE; PS00057; RIBOSOMAL_S18; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033741};
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}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 75 AA; 8675 MW; EFD418C73BD43E59 CRC64;
MATKPFFRRR KSDPFEGENA PKIDYKDTRL LQRYISERGK IVPARITAVG AKNQRKLAQA
IKRARFLALL PYAVK
//