RL4_BACTN
ID RL4_BACTN Reviewed; 208 AA.
AC Q8A477;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=BT_2726;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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}.
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; AE015928; AAO77832.1; -; Genomic_DNA.
DR RefSeq; NP_811638.1; NC_004663.1.
DR RefSeq; WP_008762035.1; NZ_UYXG01000001.1.
DR AlphaFoldDB; Q8A477; -.
DR SMR; Q8A477; -.
DR STRING; 226186.BT_2726; -.
DR PaxDb; Q8A477; -.
DR PRIDE; Q8A477; -.
DR EnsemblBacteria; AAO77832; AAO77832; BT_2726.
DR GeneID; 45362442; -.
DR GeneID; 60923897; -.
DR KEGG; bth:BT_2726; -.
DR PATRIC; fig|226186.12.peg.2769; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_10; -.
DR InParanoid; Q8A477; -.
DR OMA; PQVHILE; -.
DR Proteomes; UP000001414; 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; IBA:GO_Central.
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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..208
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129184"
FT REGION 44..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 23013 MW; 6CAE95E72431709B CRC64;
MEVNVYNIKG EDTGRKVTLN ESIFGIEPND HAIYLDVKQF MANQRQGTHK SKERSEISGS
TRKIGRQKGG GGARRGDMNS PVLVGGARVF GPKPRDYFFK LNKKVKTLAR KSALSYKVQN
NALIVVEDFV FEAPKTKDFV AMTKNLKVSD KKLLVILPEA NKNVYLSARN IEGANVQTVS
GLNTYRVLNA GVVVLTENSL KAIDNILI
