RL3_PHOLL
ID RL3_PHOLL Reviewed; 209 AA.
AC Q7MYF1;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=plu4726;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE17098.1; -; Genomic_DNA.
DR RefSeq; WP_011148795.1; NC_005126.1.
DR AlphaFoldDB; Q7MYF1; -.
DR SMR; Q7MYF1; -.
DR STRING; 243265.plu4726; -.
DR PRIDE; Q7MYF1; -.
DR EnsemblBacteria; CAE17098; CAE17098; plu4726.
DR GeneID; 24168971; -.
DR KEGG; plu:plu4726; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_6; -.
DR OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
DR BioCyc; PLUM243265:PLU_RS23405-MON; -.
DR Proteomes; UP000002514; 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..209
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000077132"
FT REGION 132..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Polar residues"
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; 22343 MW; CBEFF1E9E526CC4B CRC64;
MIGLVGKKVG MTRIFTEDGV SIPVTVIEIE DNRVTQVKEL DNDGYRAIQV TTGSKKASRV
NKPEAGHFAK AGVEAGRILR EFRLSEGEEY AVGQSISVEI FADVKKVDVT GTSKGKGFAG
TVKRWNFRTQ DASHGNSLSH RVPGSIGQNQ TPGKVFKGKK MAGQLGNERV TVQSLDVVRV
DAERNLLLVK GAVPGSTGGN LIVKPAVKA
