RL5_STAA8
ID RL5_STAA8 Reviewed; 179 AA.
AC Q2FW18;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333};
GN OrderedLocusNames=SAOUHSC_02500;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD31518.1; -; Genomic_DNA.
DR RefSeq; WP_001080824.1; NZ_LS483365.1.
DR RefSeq; YP_500967.1; NC_007795.1.
DR PDB; 4WCE; X-ray; 3.53 A; D=1-179.
DR PDB; 4WF9; X-ray; 3.43 A; D=1-179.
DR PDB; 4WFA; X-ray; 3.39 A; D=1-179.
DR PDB; 4WFB; X-ray; 3.43 A; D=1-179.
DR PDB; 5HKV; X-ray; 3.66 A; D=1-179.
DR PDB; 5HL7; X-ray; 3.55 A; D=1-179.
DR PDB; 5LI0; EM; 3.80 A; G=5-170.
DR PDB; 5ND8; EM; 3.70 A; G=1-179.
DR PDB; 5ND9; EM; 3.70 A; G=1-179.
DR PDB; 5NRG; X-ray; 3.44 A; D=1-179.
DR PDB; 5TCU; EM; 3.90 A; LK=2-167.
DR PDB; 6HMA; EM; 2.65 A; F=19-176.
DR PDB; 6YEF; EM; 3.20 A; G=1-179.
DR PDB; 7NHL; EM; 3.10 A; J=1-179.
DR PDB; 7NHM; EM; 3.10 A; J=1-179.
DR PDBsum; 4WCE; -.
DR PDBsum; 4WF9; -.
DR PDBsum; 4WFA; -.
DR PDBsum; 4WFB; -.
DR PDBsum; 5HKV; -.
DR PDBsum; 5HL7; -.
DR PDBsum; 5LI0; -.
DR PDBsum; 5ND8; -.
DR PDBsum; 5ND9; -.
DR PDBsum; 5NRG; -.
DR PDBsum; 5TCU; -.
DR PDBsum; 6HMA; -.
DR PDBsum; 6YEF; -.
DR PDBsum; 7NHL; -.
DR PDBsum; 7NHM; -.
DR AlphaFoldDB; Q2FW18; -.
DR SMR; Q2FW18; -.
DR IntAct; Q2FW18; 2.
DR STRING; 1280.SAXN108_2487; -.
DR EnsemblBacteria; ABD31518; ABD31518; SAOUHSC_02500.
DR GeneID; 3920876; -.
DR KEGG; sao:SAOUHSC_02500; -.
DR PATRIC; fig|93061.5.peg.2255; -.
DR eggNOG; COG0094; Bacteria.
DR HOGENOM; CLU_061015_2_1_9; -.
DR OMA; ERMYAFL; -.
DR PRO; PR:Q2FW18; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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; IPR020929; Ribosomal_L5_CS.
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.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..179
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000052837"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:4WFA"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:4WFB"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4WFA"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4WFA"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5NRG"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4WF9"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:6HMA"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4WF9"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6HMA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4WFA"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6HMA"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:6HMA"
SQ SEQUENCE 179 AA; 20267 MW; 3A0070FDF84DF93B CRC64;
MNRLKEKFNT EVTENLMKKF NYSSVMEVPK IDKIVVNMGV GDAVQNSKVL DNAVEELELI
TGQKPLVTKA KKSIATFRLR EGMPIGAKVT LRGERMYEFL DKLISVSLPR VRDFQGVSKK
AFDGRGNYTL GVKEQLIFPE IDYDKVSKVR GMDIVIVTTA NTDEEARELL ANFGMPFRK
