RS5_THET2
ID RS5_THET2 Reviewed; 162 AA.
AC P62665;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=30S ribosomal protein S5;
GN Name=rpsE; Synonyms=rps5; OrderedLocusNames=TT_C1311;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000250}.
CC -!- FUNCTION: Located at the back of the 30S subunit body where it
CC stabilizes the conformation of the head with respect to the body.
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and S8
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and contacts
CC protein S4. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017221; AAS81653.1; -; Genomic_DNA.
DR RefSeq; WP_008633389.1; NC_005835.1.
DR PDB; 4KVB; X-ray; 4.20 A; E=1-162.
DR PDB; 4V4I; X-ray; 3.71 A; f=1-162.
DR PDB; 4V4J; X-ray; 3.83 A; f=1-162.
DR PDB; 4V63; X-ray; 3.21 A; AE/CE=1-162.
DR PDB; 4V67; X-ray; 3.00 A; AE/CE=1-162.
DR PDB; 4V7P; X-ray; 3.62 A; AE/DE=5-155.
DR PDB; 4V83; X-ray; 3.50 A; AE/CE=5-155.
DR PDB; 4V84; X-ray; 3.40 A; AE/CE=5-155.
DR PDB; 4V9J; X-ray; 3.86 A; AE/CE=5-155.
DR PDB; 4V9K; X-ray; 3.50 A; AE/CE=5-155.
DR PDB; 4V9L; X-ray; 3.50 A; AE/CE=5-155.
DR PDB; 4V9M; X-ray; 4.00 A; AE/CE=5-155.
DR PDB; 4V9N; X-ray; 3.40 A; AE/CE=5-155.
DR PDB; 4V9Q; X-ray; 3.40 A; BE/DE=5-155.
DR PDB; 4W29; X-ray; 3.80 A; AE/CE=5-155.
DR PDB; 4XEJ; X-ray; 3.80 A; AS05/BS05=5-155.
DR PDB; 5J4D; X-ray; 3.10 A; NA/SC=1-162.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; P62665; -.
DR SMR; P62665; -.
DR IntAct; P62665; 4.
DR STRING; 262724.TT_C1311; -.
DR EnsemblBacteria; AAS81653; AAS81653; TT_C1311.
DR GeneID; 3169827; -.
DR KEGG; tth:TT_C1311; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_2_0; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 1505038at2; -.
DR EvolutionaryTrace; P62665; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005712; Ribosomal_S5_bac-type.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..162
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131620"
FT DOMAIN 7..70
FT /note="S5 DRBM"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4V9N"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4V9Q"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 162 AA; 17557 MW; BE3367CB619E68D2 CRC64;
MPETDFEEKM ILIRRTARMQ AGGRRFRFGA LVVVGDRQGR VGLGFGKAPE VPLAVQKAGY
YARRNMVEVP LQNGTIPHEI EVEFGASKIV LKPAAPGTGV IAGAVPRAIL ELAGVTDILT
KELGSRNPIN IAYATMEALR QLRTKADVER LRKGEAHAQA QG
