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Database: UniProt
Entry: A0A1T1ICY3_9PSED
LinkDB: A0A1T1ICY3_9PSED
Original site: A0A1T1ICY3_9PSED 
ID   A0A1T1ICY3_9PSED        Unreviewed;        76 AA.
AC   A0A1T1ICY3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=MF4836_05930 {ECO:0000313|EMBL:OOV99772.1};
OS   Pseudomonas sp. MF4836.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV99772.1, ECO:0000313|Proteomes:UP000190183};
RN   [1] {ECO:0000313|Proteomes:UP000190183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA   Fagerlund A.;
RT   "Genome sequencing of bacteria from food industry.";
RL   Submitted (FEB-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}.
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:OOV99772.1}.
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DR   EMBL; MVOL01000002; OOV99772.1; -; Genomic_DNA.
DR   RefSeq; WP_002551829.1; NZ_MVOL01000002.1.
DR   AlphaFoldDB; A0A1T1ICY3; -.
DR   SMR; A0A1T1ICY3; -.
DR   STRING; 1960827.MF4836_05930; -.
DR   GeneID; 78555437; -.
DR   Proteomes; UP000190183; 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   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   76 AA;  8917 MW;  D1998415EBF38E99 CRC64;
     MARFFRRRKF CRFTAEDVKE IDYKDLNTLK AYVSETGKIV PSRITGTKAR YQRQLATAIK
     RARFLALLAY TDSHGR
//
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