ID F0QR63_MYCSL Unreviewed; 162 AA.
AC F0QR63;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Small ribosomal subunit protein uS13 {ECO:0000256|HAMAP-Rule:MF_01315};
GN Name=rpsM {ECO:0000256|HAMAP-Rule:MF_01315,
GN ECO:0000313|EMBL:ADX97983.1};
GN OrderedLocusNames=MSU_0447 {ECO:0000313|EMBL:ADX97983.1};
OS Mycoplasma suis (strain Illinois).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=768700 {ECO:0000313|EMBL:ADX97983.1, ECO:0000313|Proteomes:UP000007484};
RN [1] {ECO:0000313|EMBL:ADX97983.1, ECO:0000313|Proteomes:UP000007484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Illinois {ECO:0000313|EMBL:ADX97983.1,
RC ECO:0000313|Proteomes:UP000007484};
RX PubMed=21317328; DOI=10.1128/JB.00133-11;
RA Messick J.B., Santos A.P., Guimaraes A.M.;
RT "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL J. Bacteriol. 193:2068-2069(2011).
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; CP002525; ADX97983.1; -; Genomic_DNA.
DR RefSeq; WP_013609862.1; NC_015155.1.
DR AlphaFoldDB; F0QR63; -.
DR STRING; 768700.MSU_0447; -.
DR KEGG; mss:MSU_0447; -.
DR HOGENOM; CLU_103849_1_2_14; -.
DR Proteomes; UP000007484; 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 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; PS50159; RIBOSOMAL_S13_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007484};
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01315};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01315};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01315}.
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 162 AA; 18538 MW; 6EE3668B8E03EBE5 CRC64;
MARILGVILP DKKELFVALT KIYGIGLTTS KKIIQYWVLN KVISENKLTE AEKSKLEVYM
KKRVYSLSSE ELASLSQAIV KLQSIQEEVP EVSSFFKDRL LLEGDLRKKI SDDLTNLKEI
ASYVGLRHRR NLPVHGQRTR TNARTRKGPR KTVANKKIEG KK
//
