RL3_BORBU
ID RL3_BORBU Reviewed; 206 AA.
AC P94267; O51432;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=BB_0478;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Perlee L., Qi H., Schwartz I.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR EMBL; U78193; AAB36822.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66864.1; -; Genomic_DNA.
DR PIR; E70159; E70159.
DR RefSeq; NP_212612.1; NC_001318.1.
DR AlphaFoldDB; P94267; -.
DR SMR; P94267; -.
DR STRING; 224326.BB_0478; -.
DR PRIDE; P94267; -.
DR EnsemblBacteria; AAC66864; AAC66864; BB_0478.
DR KEGG; bbu:BB_0478; -.
DR PATRIC; fig|224326.49.peg.869; -.
DR HOGENOM; CLU_044142_4_1_12; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000001807; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..206
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000077070"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 164
FT /note="A -> G (in Ref. 1; AAC66864)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> P (in Ref. 1; AAB36822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 22226 MW; C39092C881F1519A CRC64;
MLGLIGKKVG MTQIFQKNGI VVPVTVIEFQ PNYIIGKKTV DRDGYSALIA GSVDLKSSKV
SKPIKGQYKS LKDIEPKRYV IELKGLDGYD AGDEIKVDVF KSVKYVDVTG TTKGKGFQGA
MKRHNFSGGP SSHGSKFHRH LGGTGQATTP ARTFKGTKMA GRMAGNQQTI QNLEVVLIDE
EKRALLVKGA VPGAKGSFVV VKKSKK
