RL4_DESAH
ID RL4_DESAH Reviewed; 207 AA.
AC C0Q9X2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=HRM2_36250;
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN16690.1; -; Genomic_DNA.
DR RefSeq; WP_015905440.1; NC_012108.1.
DR AlphaFoldDB; C0Q9X2; -.
DR SMR; C0Q9X2; -.
DR STRING; 177437.HRM2_36250; -.
DR EnsemblBacteria; ACN16690; ACN16690; HRM2_36250.
DR KEGG; dat:HRM2_36250; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_7; -.
DR OMA; PQVHILE; -.
DR OrthoDB; 1572673at2; -.
DR Proteomes; UP000000442; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..207
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000214567"
FT REGION 43..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22717 MW; 21357646BD9EFF03 CRC64;
MAAVDVLNRS GEKVSEAFLA DEVFSIPVKK SVLHDVVRMQ LARRRSGTAK SKGRSEVSGS
TRKLYRQKGT GNARSGSVKS PLRRGGGVIF GPAPRSYAYA IPKKVRALAL KMALSSKLAA
NELSVIDTFA MDSIKTKEFD SIIDHLGLKN TLIVIDGDDR NLVLSARNIP DVKVIRTEGL
NVYDILKYDN LLLIESAIKE IEGRFTR
