RL4_MYCS2
ID RL4_MYCS2 Reviewed; 215 AA.
AC A0QSD2; I7G5M3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN OrderedLocusNames=MSMEG_1437, MSMEI_1401;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(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; CP000480; ABK72271.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37874.1; -; Genomic_DNA.
DR RefSeq; WP_011727671.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885820.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; E=1-215.
DR PDB; 5O61; EM; 3.31 A; E=1-215.
DR PDB; 5XYM; EM; 3.08 A; E=1-215.
DR PDB; 5ZEB; EM; 3.40 A; E=1-215.
DR PDB; 5ZEP; EM; 3.40 A; E=1-215.
DR PDB; 5ZET; EM; 3.20 A; E=1-215.
DR PDB; 6DZI; EM; 3.46 A; E=2-210.
DR PDB; 6DZP; EM; 3.42 A; E=2-215.
DR PDBsum; 5O60; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5XYM; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZET; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZP; -.
DR AlphaFoldDB; A0QSD2; -.
DR SMR; A0QSD2; -.
DR IntAct; A0QSD2; 3.
DR STRING; 246196.MSMEI_1401; -.
DR PRIDE; A0QSD2; -.
DR EnsemblBacteria; ABK72271; ABK72271; MSMEG_1437.
DR EnsemblBacteria; AFP37874; AFP37874; MSMEI_1401.
DR GeneID; 66732896; -.
DR KEGG; msg:MSMEI_1401; -.
DR KEGG; msm:MSMEG_1437; -.
DR PATRIC; fig|246196.19.peg.1423; -.
DR eggNOG; COG0088; Bacteria.
DR OMA; PQVHILE; -.
DR OrthoDB; 1572673at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..215
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000052444"
FT REGION 43..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6DZP"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:5XYM"
SQ SEQUENCE 215 AA; 22885 MW; CC681F99FC2C5F56 CRC64;
MTLKVDVKTP AGKTDGSVEL PAELFDVEPN IALMHQVVTA QLAAKRQGTH STKTRGEVSG
GGKKPYRQKG TGRARQGSTR APQFTGGGTV HGPKPRDYSQ RTPKKMIAAA LRGALSDRAR
NDRIHAVTEL VEGQTPSTKS AKTFLGTLTE NKKVLVVIGR TDEVGAKSVR NLPGVHVISP
DQLNTYDVLN ADDVVFSVEA LNAYISANSK EGASV
