ID   RS5_THETH               Reviewed;         162 AA.
AC   P27152;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000305};
DE   AltName: Full=30S ribosomal protein S5;
GN   Name=rpsE; Synonyms=rps5;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RX   PubMed=9249063; DOI=10.1016/s0378-1119(97)00072-3;
RA   Vysotskaya V.S., Shcherbakov D.V., Garber M.B.;
RT   "Sequencing and analysis of the Thermus thermophilus ribosomal protein gene
RT   cluster equivalent to the spectinomycin operon.";
RL   Gene 193:23-30(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-26.
RC   STRAIN=VK1;
RX   PubMed=1637860; DOI=10.1016/0300-9084(92)90110-z;
RA   Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V.,
RA   Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A.,
RA   Svensson L.A.;
RT   "Ribosomal proteins from Thermus thermophilus for structural
RT   investigations.";
RL   Biochimie 74:327-336(1992).
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}.
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DR   EMBL; X90765; CAA62290.1; -; Genomic_DNA.
DR   PIR; A48401; A48401.
DR   RefSeq; WP_008633389.1; NZ_LR027517.1.
DR   PDB; 4V8X; X-ray; 3.35 A; AE/CE=1-162.
DR   PDBsum; 4V8X; -.
DR   AlphaFoldDB; P27152; -.
DR   SMR; P27152; -.
DR   GeneID; 3169827; -.
DR   OMA; GIKDVWT; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_uS5_B; 1.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR000851; Ribosomal_uS5.
DR   InterPro; IPR005712; Ribosomal_uS5_bac-type.
DR   InterPro; IPR005324; Ribosomal_uS5_C.
DR   InterPro; IPR013810; Ribosomal_uS5_N.
DR   InterPro; IPR018192; Ribosomal_uS5_N_CS.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01021; rpsE_bact; 1.
DR   PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR   PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1637860"
FT   CHAIN           2..162
FT                   /note="Small ribosomal subunit protein uS5"
FT                   /id="PRO_0000131622"
FT   DOMAIN          6..69
FT                   /note="S5 DRBM"
FT   CONFLICT        2
FT                   /note="P -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        5
FT                   /note="D -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="R -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..20
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          23..35
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          37..50
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   HELIX           51..63
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   HELIX           104..110
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   HELIX           128..139
FT                   /evidence="ECO:0007829|PDB:4V8X"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:4V8X"
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
//