RL3_ERYLH
ID RL3_ERYLH Reviewed; 289 AA.
AC Q2N9B1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=ELI_08190;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000157; ABC63730.1; -; Genomic_DNA.
DR RefSeq; WP_011414562.1; NC_007722.1.
DR AlphaFoldDB; Q2N9B1; -.
DR SMR; Q2N9B1; -.
DR STRING; 314225.ELI_08190; -.
DR EnsemblBacteria; ABC63730; ABC63730; ELI_08190.
DR KEGG; eli:ELI_08190; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_2_0_5; -.
DR OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
DR Proteomes; UP000008808; 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; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..289
FT /note="50S ribosomal protein L3"
FT /id="PRO_1000052047"
FT REGION 230..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 289 AA; 30935 MW; 43A2088641D75B5C CRC64;
MRTGVIAKKV GMTRLFQEDG RHVPVTVLAL EDCQVVSQRT QERDGYFALQ VGSGVAKQKN
VAKPQREAFA KAEVGLKMKV AEFRVEGEDG LLPVGAAISA EHFIAGQKVD ITGYTQGKGF
AGAMKRWGFG GLRATHGVSI SHRSHGSTGN RQDPGRVFKG KKMAGHMGDR QRTQQNLEVV
RTDPERGLIF VKGSVPGTKN SWMLIRDAVK LPLPEGVPFP GAVVEKNAPA KEADAPAADE
QKLDDVANEE AVVEEKAADK QTNDTAAPAE ETPAEEAPKA DDSDAGKEG