ID   A0A2T0Z1F6_9ACTN        Unreviewed;       123 AA.
AC   A0A2T0Z1F6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CLV47_13123 {ECO:0000313|EMBL:PRZ30189.1};
OS   Antricoccus suffuscus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Antricoccaceae; Antricoccus.
OX   NCBI_TaxID=1629062 {ECO:0000313|EMBL:PRZ30189.1, ECO:0000313|Proteomes:UP000237752};
RN   [1] {ECO:0000313|EMBL:PRZ30189.1, ECO:0000313|Proteomes:UP000237752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100065 {ECO:0000313|EMBL:PRZ30189.1,
RC   ECO:0000313|Proteomes:UP000237752};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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}.
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:PRZ30189.1}.
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DR   EMBL; PVUE01000031; PRZ30189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0Z1F6; -.
DR   OrthoDB; 9803610at2; -.
DR   Proteomes; UP000237752; 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:UP000237752};
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..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..123
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   123 AA;  13944 MW;  C8BB667507AE894F CRC64;
     MARISGVDLP REKRTVIALT YIFGVGRTSS EKALEATGVD GSIRVKDLTD EDLIKLREYI
     DGNLRVEGDL RREVQADIRR KMEIGCYQGI RHRRGLPVHG QRTRTNARSR KGPKKTISGK
     KKK
//