RL5_MYCS2
ID RL5_MYCS2 Reviewed; 187 AA.
AC A0QSG1; I7G5P8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333};
GN OrderedLocusNames=MSMEG_1467, MSMEI_1431;
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: This is 1 of the proteins that binds and probably mediates
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. In the 70S ribosome it contacts
CC protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC this bridge is implicated in subunit movement. Contacts the P site
CC tRNA; the 5S rRNA and some of its associated proteins might help
CC stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01333}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA.
CC Forms a bridge to the 30S subunit in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR EMBL; CP000480; ABK75083.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37904.1; -; Genomic_DNA.
DR RefSeq; WP_003892854.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885849.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; F=1-187.
DR PDB; 5O61; EM; 3.31 A; F=1-187.
DR PDB; 5XYM; EM; 3.08 A; F=1-187.
DR PDB; 5ZEB; EM; 3.40 A; F=1-187.
DR PDB; 5ZEP; EM; 3.40 A; F=1-187.
DR PDB; 5ZET; EM; 3.20 A; F=1-187.
DR PDB; 6DZI; EM; 3.46 A; F=6-187.
DR PDB; 6DZP; EM; 3.42 A; F=2-187.
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; A0QSG1; -.
DR SMR; A0QSG1; -.
DR IntAct; A0QSG1; 3.
DR STRING; 246196.MSMEI_1431; -.
DR PRIDE; A0QSG1; -.
DR EnsemblBacteria; ABK75083; ABK75083; MSMEG_1467.
DR EnsemblBacteria; AFP37904; AFP37904; MSMEI_1431.
DR GeneID; 66732924; -.
DR KEGG; msg:MSMEI_1431; -.
DR KEGG; msm:MSMEG_1467; -.
DR PATRIC; fig|246196.19.peg.1452; -.
DR eggNOG; COG0094; Bacteria.
DR OMA; ERMYAFL; -.
DR OrthoDB; 1456375at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1440.10; -; 1.
DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR020930; Ribosomal_L5_bac-type.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..187
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000052777"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5O60"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:5XYM"
SQ SEQUENCE 187 AA; 21122 MW; E7F306D071E5C282 CRC64;
MTTTEKALPR LKQRYREEIR EALQQEFNYA NVMQIPGVVK VVVNMGVGDA ARDAKLINGA
INDLALITGQ KPEVRRARKS IAQFKLREGM PIGARVTLRG DRMWEFLDRL ISIALPRIRD
FRGLSPKQFD GTGNYTFGLN EQSMFHEIDV DSIDRPRGMD ITVVTTATND AEGRALLRAL
GFPFKEN
