ID   RL3_BORAP               Reviewed;         206 AA.
AC   Q0SN29; G0ISC2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325};
GN   OrderedLocusNames=BAPKO_0506, BafPKo_0495;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01749.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69703.1; -; Genomic_DNA.
DR   RefSeq; WP_011601050.1; NC_017238.1.
DR   AlphaFoldDB; Q0SN29; -.
DR   SMR; Q0SN29; -.
DR   STRING; 390236.BafPKo_0495; -.
DR   EnsemblBacteria; AEL69703; AEL69703; BafPKo_0495.
DR   KEGG; baf:BAPKO_0506; -.
DR   KEGG; bafz:BafPKo_0495; -.
DR   PATRIC; fig|390236.22.peg.475; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_4_1_12; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000005216; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..206
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000052014"
FT   REGION          127..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  22153 MW;  6AC98200FE786B94 CRC64;
     MLGLIGKKVG MTQIFQKNGI VVPVTVIEFQ PNYIIGKKTV DRDGYSALIA GSVDLKGSKV
     SKPIKGQYKS LKDIEPKKYV IELKGLDGYD AGDEIKVDVF KSVKYVDVTG TTKGKGFQGA
     MKRHNFSGGP SSHGSKFHRH LGGTGQATTP ARTFKGTKMA GRMGGNQQTI QNLEVVLINE
     EKRAILVKGA VPGAKGSFVV VKKSKK