RL4_BORAP
ID RL4_BORAP Reviewed; 209 AA.
AC Q0SN28; G0ISC3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN OrderedLocusNames=BAPKO_0507, BafPKo_0496;
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, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR EMBL; CP000395; ABH01750.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69704.1; -; Genomic_DNA.
DR RefSeq; WP_011601051.1; NC_017238.1.
DR AlphaFoldDB; Q0SN28; -.
DR SMR; Q0SN28; -.
DR STRING; 390236.BafPKo_0496; -.
DR EnsemblBacteria; AEL69704; AEL69704; BafPKo_0496.
DR KEGG; baf:BAPKO_0507; -.
DR KEGG; bafz:BafPKo_0496; -.
DR PATRIC; fig|390236.22.peg.476; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_12; -.
DR OMA; PQVHILE; -.
DR OrthoDB; 1572673at2; -.
DR Proteomes; UP000005216; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..209
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000052359"
FT REGION 46..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23691 MW; 3693E80B55DDCF13 CRC64;
MERKVFSKDG KEIRTINLDD RVFNIEISHG SIYNAIKNEL SNLRVGTSST KTRSEVRGSS
KKPWKQKGTG RARVGTRRNP VWIGGGIALG PKPRDYSYRL PKKVKRLAFK SVLSLRASDE
NNFKVIENFN IESGKTKDLA LIIKNFASFN GKVVILLGND DQMIKRAGKN IRDLKILSFD
KLRVVDLFYA KNLIALESAV NKLNEFYVK
