RL4_CHLPM
ID RL4_CHLPM Reviewed; 208 AA.
AC A4SCR0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Cvib_0247;
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 / 1930;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000607; ABP36269.1; -; Genomic_DNA.
DR RefSeq; WP_011889498.1; NC_009337.1.
DR AlphaFoldDB; A4SCR0; -.
DR SMR; A4SCR0; -.
DR STRING; 290318.Cvib_0247; -.
DR EnsemblBacteria; ABP36269; ABP36269; Cvib_0247.
DR KEGG; pvi:Cvib_0247; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_10; -.
DR OMA; PQVHILE; -.
DR OrthoDB; 1572673at2; -.
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..208
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000086531"
FT REGION 45..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 22802 MW; 217248122D037538 CRC64;
MELKVLTTAG TESGEVVTLR DDIFGAEVSE HAVYLDVKSI LANRRQGTHK SKTRAEVRGG
GRKPYRQKGT GNARQGSTRS PLMVGGGTIF GPTPHGYDQK VNKKVKALAR RSAFSSKAQD
GRILVVEDFK LDEIKTKPFA AILKNLGLDE KKTLMLTPEY NVIITRSGKN IQTVNIMSAE
KASTYDILNS HTVLFQKAAL KKIEETLG