ID K4L3L8_9FIRM Unreviewed; 123 AA.
AC K4L3L8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ECO:0000313|EMBL:AFV05877.1};
GN ORFNames=DCF50_p1875 {ECO:0000313|EMBL:AFV05877.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV05877.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV05877.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV05877.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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; CP003870; AFV05877.1; -; Genomic_DNA.
DR RefSeq; WP_015043919.1; NC_018867.1.
DR AlphaFoldDB; K4L3L8; -.
DR STRING; 1131462.DCF50_p1875; -.
DR KEGG; dec:DCF50_p1875; -.
DR PATRIC; fig|1131462.4.peg.1892; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_9; -.
DR Proteomes; UP000000482; 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: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:UP000000482};
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};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01315}.
FT REGION 95..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 14028 MW; 0A0B6D2CD9EFEAF0 CRC64;
MARIAGVDIP RDKRVEVALT YIYGIGNSQS KKILTKTQIN PDTRVKDLTD DEVAKIRETI
DKEYKVEGDL RREVSLNIKR LMEIGSYRGL RHRRGLPVRG QRTKTNARTR KGPARAIGGK
KKK
//
