RS3_AKKM8
ID RS3_AKKM8 Reviewed; 229 AA.
AC B2UMT3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=Amuc_0297;
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-
CC Rule:MF_01309}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01309}.
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DR EMBL; CP001071; ACD04139.1; -; Genomic_DNA.
DR RefSeq; WP_012419354.1; NC_010655.1.
DR AlphaFoldDB; B2UMT3; -.
DR SMR; B2UMT3; -.
DR STRING; 349741.Amuc_0297; -.
DR EnsemblBacteria; ACD04139; ACD04139; Amuc_0297.
DR GeneID; 60879775; -.
DR KEGG; amu:Amuc_0297; -.
DR eggNOG; COG0092; Bacteria.
DR HOGENOM; CLU_058591_0_2_0; -.
DR OMA; KTNPIGN; -.
DR OrthoDB; 1132353at2; -.
DR BioCyc; AMUC349741:G1GBX-339-MON; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..229
FT /note="30S ribosomal protein S3"
FT /id="PRO_1000140917"
FT DOMAIN 39..109
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25873 MW; C257B0978DA1FA5D CRC64;
MGQKVNPIGF RLAVNKDWRS KWYATGQDYA TKLHEDLVMR KYIKEQLMSA AVSSIVIERA
WNSVRITVHT ARPGLVIGRK GEEIEKIRQY LQGLCGASTQ VNIDIVEIRS PETDAQLIAE
NVAVQLERRV SFRRAMKRAV QVAMERGADG IRIRCAGRLG GADIARAEWY REGKVPLQTL
RTPIDYGFAE ARTLYGIIGV KCWVNKRDEV VSQQNSRPSG PRGPRRPRA
