ID A0A1Y4RNG7_9FIRM Unreviewed; 122 AA.
AC A0A1Y4RNG7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=B5E84_06825 {ECO:0000313|EMBL:OUQ18999.1};
OS Lachnoclostridium sp. An14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965562 {ECO:0000313|EMBL:OUQ18999.1, ECO:0000313|Proteomes:UP000196089};
RN [1] {ECO:0000313|Proteomes:UP000196089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An14 {ECO:0000313|Proteomes:UP000196089};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
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:OUQ18999.1}.
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DR EMBL; NFLE01000009; OUQ18999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4RNG7; -.
DR OrthoDB; 9803610at2; -.
DR Proteomes; UP000196089; 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:UP000196089};
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..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13737 MW; 8F199F248CF07442 CRC64;
MARISGVDLP REKRVEIGLT YIYGIGRASA NRILAEAGVN PDTRVKDLTD DEVKKISAVI
AETQVVEGDL RREIAMNIKR LQEIGCYRGI RHRRSLPVRG QKTKTNARTR KGPRKTVANK
KK
//
