RL3_PSEU2
ID RL3_PSEU2 Reviewed; 211 AA.
AC Q4ZMP4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Psyr_4548;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY39578.1; -; Genomic_DNA.
DR RefSeq; WP_002555490.1; NC_007005.1.
DR RefSeq; YP_237616.1; NC_007005.1.
DR AlphaFoldDB; Q4ZMP4; -.
DR SMR; Q4ZMP4; -.
DR STRING; 205918.Psyr_4548; -.
DR EnsemblBacteria; AAY39578; AAY39578; Psyr_4548.
DR GeneID; 61872121; -.
DR GeneID; 64445580; -.
DR KEGG; psb:Psyr_4548; -.
DR PATRIC; fig|205918.7.peg.4687; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_6; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000000426; 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..211
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000241392"
FT MOD_RES 150
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 211 AA; 22593 MW; 8F552990175B00C6 CRC64;
MTIGVVGRKC GMTRIFTEEG VSIPVTVIEI EPNRVTQFKT EETDGYRAVQ VTVGERRASR
VTAAQAGHFA KANVAAGRTV MEFRLEEGDY QAGDQINAEI FAAGQLVDVT GQSKGKGFQG
TIKRWNFRGQ DNTHGNSVSH RVPGSIGQCQ TPGRVFKGKK MSGHMGAERV TVQSLEVVRV
DAERNLLLVK GAVPGATGGN LVVRPAAKAR G