RL3_ROSDO
ID RL3_ROSDO Reviewed; 286 AA.
AC Q16AF4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=RD1_1399;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG31039.1; -; Genomic_DNA.
DR RefSeq; WP_011567659.1; NZ_FOOO01000013.1.
DR AlphaFoldDB; Q16AF4; -.
DR SMR; Q16AF4; -.
DR STRING; 375451.RD1_1399; -.
DR EnsemblBacteria; ABG31039; ABG31039; RD1_1399.
DR KEGG; rde:RD1_1399; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_2_0_5; -.
DR OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
DR Proteomes; UP000007029; 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; 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.
PE 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..286
FT /note="50S ribosomal protein L3"
FT /id="PRO_1000052129"
FT REGION 246..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..286
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 286 AA; 29662 MW; A7408BF3B77B6E1B CRC64;
MLRSGVIAKK VGMTRLFMED GKQIPVTVLQ LDKLQVVAQR TSEKDGYSAV QLGAGTAKAK
RTSQAMRGHF AAAKVEPKRK VAEFRVDPEN LIGVGEEITA NHYFEGQFVD VAGTSIGKGF
AGAMKRHNFG GLRASHGVSI SHRSHGSTGQ CQDPGKVFKG KKMAGHMGAA RVTTQNLQVV
RTDANRGLIM VKGAVPGSKG GWVTVKDAVK KPFPENAILP AALKSAAEEA EKAAEAAAAA
AAAEAEAAAA AAAAEEQAAM EAAEAAEAKT DTVAEAEAAE KKEGDA