RL3_BRUO2
ID RL3_BRUO2 Reviewed; 237 AA.
AC A5VR06;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=BOV_1196;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(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; CP000708; ABQ61627.1; -; Genomic_DNA.
DR RefSeq; WP_004688461.1; NC_009505.1.
DR AlphaFoldDB; A5VR06; -.
DR SMR; A5VR06; -.
DR EnsemblBacteria; ABQ61627; ABQ61627; BOV_1196.
DR GeneID; 45124601; -.
DR GeneID; 55590908; -.
DR KEGG; bov:BOV_1196; -.
DR HOGENOM; CLU_044142_2_0_5; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000006383; Chromosome I.
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..237
FT /note="50S ribosomal protein L3"
FT /id="PRO_1000052017"
FT REGION 133..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 237 AA; 25078 MW; C893B7EBC6E50AE5 CRC64;
MRSGVIAQKL GMTRVYNDAG EHVPVTVLRM ENCHVVAQRT VEKNGYTAVQ LGVGMAKVKN
TSKAMRGHFA KAEVEPKAKL AEFRVSPDNL LEVGVEITAE HFVAGQKVDV TGTSIGKGFA
GVMKRHNFGG HRASHGNSIT HRSHGSTGQR QDPGKVFKGK KMAGHMGQTR VTTQNIEVVS
TDSDRGLILV RGAVPGSKGA WILVRDAVKA SLPENAPKPA GLRAGAKAEA AATEGAE