ID A0A5Q0EL98_9GAMM Unreviewed; 118 AA.
AC A0A5Q0EL98;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 08-NOV-2023, entry version 12.
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:QFY90065.1};
GN ORFNames=D5125_11550 {ECO:0000313|EMBL:QFY90065.1};
OS gamma proteobacterium SS-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=947516 {ECO:0000313|EMBL:QFY90065.1, ECO:0000313|Proteomes:UP000326736};
RN [1] {ECO:0000313|Proteomes:UP000326736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-5 {ECO:0000313|Proteomes:UP000326736};
RA Geurink C.J., Bazylinski D.A., Lefevre C.T.;
RT "Comparative genomic analysis of magnetotactic Gammaproteobacteria reveals
RT a new group of genes conserved in magnetotactic bacteria with likely
RT involvment in the mineralization of magnetite magnetosomes.";
RL Submitted (SEP-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; CP032508; QFY90065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0EL98; -.
DR OrthoDB; 9803610at2; -.
DR Proteomes; UP000326736; 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:UP000326736};
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 91..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 118 AA; 13341 MW; 925F26AD964263F1 CRC64;
MARIAGVNIP DKKHAVIALT SIYGVGRTRA GLICAAVGIE PHRKIQELNE EDLDRIRGEV
AKFAVEGDLR REVSMNIKRL MDLGCNRGIR HRRGLPLRGQ RTRTNARTRK GPRRPIKR
//
