RL3_YERE8
ID RL3_YERE8 Reviewed; 209 AA.
AC A1JS47;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=YE3923;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR EMBL; AM286415; CAL13942.1; -; Genomic_DNA.
DR RefSeq; WP_004709250.1; NC_008800.1.
DR RefSeq; YP_001008068.1; NC_008800.1.
DR AlphaFoldDB; A1JS47; -.
DR SMR; A1JS47; -.
DR STRING; 393305.YE3923; -.
DR EnsemblBacteria; CAL13942; CAL13942; YE3923.
DR GeneID; 61905815; -.
DR GeneID; 67421345; -.
DR KEGG; yen:YE3923; -.
DR PATRIC; fig|393305.7.peg.4173; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_6; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000000642; Chromosome.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..209
FT /note="50S ribosomal protein L3"
FT /id="PRO_1000052167"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 209 AA; 22274 MW; 8A3CA7D299E34060 CRC64;
MIGLVGKKVG MTRIFTEDGV SIPVTVIEIE ANRVTQVKSL ENDGYRAVQV TTGAKKANRV
TKPEAGHFAK AGVEAGRGLW EFRLPEGQEF TAGQEISVEI FADVKKVDVT GTSKGKGFAG
TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ TPGKVFKGKK MAGHLGDERV TVQSLDVVRV
DAERNLLLVK GAVPGATGGN LIVKPAVKA