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Database: UniProt
Entry: A0A160KR64_9MICO
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ID   A0A160KR64_9MICO        Unreviewed;       126 AA.
AC   A0A160KR64;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Small ribosomal subunit protein uS13 {ECO:0000256|ARBA:ARBA00035166, ECO:0000256|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000256|HAMAP-Rule:MF_01315};
GN   ORFNames=A6122_0608 {ECO:0000313|EMBL:AND15764.1}, C5C18_12475
GN   {ECO:0000313|EMBL:PPG05715.1};
OS   Rathayibacter tritici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=33888 {ECO:0000313|EMBL:AND15764.1, ECO:0000313|Proteomes:UP000077071};
RN   [1] {ECO:0000313|EMBL:AND15764.1, ECO:0000313|Proteomes:UP000077071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND15764.1,
RC   ECO:0000313|Proteomes:UP000077071};
RA   Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT   "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PPG05715.1, ECO:0000313|Proteomes:UP000239776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG05715.1,
RC   ECO:0000313|Proteomes:UP000239776};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Located at the top of the head of the 30S subunit, it
CC       contacts several helices of the 16S rRNA. In the 70S ribosome it
CC       contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit
CC       (bridge B1b), connecting the 2 subunits; these bridges are implicated
CC       in subunit movement. Contacts the tRNAs in the A and P-sites.
CC       {ECO:0000256|HAMAP-Rule:MF_01315}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose heterodimer
CC       with protein S19. Forms two bridges to the 50S subunit in the 70S
CC       ribosome. {ECO:0000256|HAMAP-Rule:MF_01315}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000256|ARBA:ARBA00008080, ECO:0000256|HAMAP-Rule:MF_01315,
CC       ECO:0000256|RuleBase:RU003830}.
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DR   EMBL; CP015515; AND15764.1; -; Genomic_DNA.
DR   EMBL; PSUO01000023; PPG05715.1; -; Genomic_DNA.
DR   RefSeq; WP_068251511.1; NZ_PSWT01000036.1.
DR   AlphaFoldDB; A0A160KR64; -.
DR   STRING; 33888.A6122_0608; -.
DR   GeneID; 49819174; -.
DR   KEGG; rtn:A6122_0608; -.
DR   PATRIC; fig|33888.3.peg.679; -.
DR   OrthoDB; 9803610at2; -.
DR   Proteomes; UP000077071; Chromosome.
DR   Proteomes; UP000239776; 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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 4.10.910.10; 30s ribosomal protein s13, domain 2; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; Rbsml_uS13_C.
DR   InterPro; IPR001892; Ribosomal_uS13.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR019980; Ribosomal_uS13_bac-type.
DR   InterPro; IPR018269; Ribosomal_uS13_CS.
DR   NCBIfam; TIGR03631; uS13_bact; 1.
DR   PANTHER; PTHR10871; 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18; 1.
DR   PANTHER; PTHR10871:SF1; 37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL; 1.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077071};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01315}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01315}.
FT   REGION          93..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..126
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   126 AA;  14203 MW;  1FE021EDBB7098E2 CRC64;
     MARLAGVDIP REKRVEVALT YIYGVGRTRA LKTLSDTGID GNIRVKDLSD DQLVSLRDYI
     EGNYKVEGDL RREVAADIRR KVEIGSYEGL RHRRGLPVRG QRTKTNARTR KGPKRTVAGK
     KKAGRK
//
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