RL4_HELAH
ID RL4_HELAH Reviewed; 215 AA.
AC Q17ZD7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Hac_0137;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ98989.1; -; Genomic_DNA.
DR RefSeq; WP_011577109.1; NC_008229.1.
DR AlphaFoldDB; Q17ZD7; -.
DR SMR; Q17ZD7; -.
DR STRING; 382638.Hac_0137; -.
DR EnsemblBacteria; CAJ98989; CAJ98989; Hac_0137.
DR KEGG; hac:Hac_0137; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_7; -.
DR OMA; HVRINKK; -.
DR OrthoDB; 1572673at2; -.
DR BioCyc; HACI382638:HAC_RS00585-MON; -.
DR Proteomes; UP000000775; 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..215
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000052414"
FT REGION 46..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 215 AA; 24100 MW; 5D65A39D126DBDF9 CRC64;
MSKAIVLDSH LKEKGSMELP KRYEGINSHN LYLYVKHYLS SVRANTAKSK NRAEVSGGGR
KPWAQKGGGR ARAGSITSPV FVGGGVSHGA TNNRNYNLKI NKKQKRLALE YALEEKAQAN
KLFVVEKIAI KGVVEYNKRK HLAKEANKMF QALEQRDTLF VCMNMDEYTE LAFSNLKKCL
VIDVSELNAY LLAAFSSVVM EEVAFQHVVQ DKTEE