RS2_THET2
ID RS2_THET2 Reviewed; 256 AA.
AC P62662;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=30S ribosomal protein S2;
GN Name=rpsB; Synonyms=rps2; OrderedLocusNames=TT_C0509;
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 [GENOMIC DNA].
RX PubMed=11296217; DOI=10.1093/emboj/20.8.1829;
RA Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H.,
RA Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A.,
RA Franceschi F.;
RT "Crystal structures of complexes of the small ribosomal subunit with
RT tetracycline, edeine and IF3.";
RL EMBO J. 20:1829-1839(2001).
RN [2]
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: Spans the head-body hinge region of the 30S subunit. Is
CC loosely associated with the 30S subunit (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S8 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000305}.
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DR EMBL; AJ409329; CAC35061.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS80857.1; -; Genomic_DNA.
DR RefSeq; WP_011172954.1; NC_005835.1.
DR PDB; 4KVB; X-ray; 4.20 A; B=1-256.
DR PDB; 4V4G; X-ray; 11.50 A; B=7-240.
DR PDB; 4V4I; X-ray; 3.71 A; c=1-256.
DR PDB; 4V4J; X-ray; 3.83 A; c=1-256.
DR PDB; 4V63; X-ray; 3.21 A; AB/CB=1-256.
DR PDB; 4V67; X-ray; 3.00 A; AB/CB=1-256.
DR PDB; 4V7P; X-ray; 3.62 A; AB/DB=7-240.
DR PDB; 4V83; X-ray; 3.50 A; AB/CB=7-240.
DR PDB; 4V84; X-ray; 3.40 A; AB/CB=7-240.
DR PDB; 4V9J; X-ray; 3.86 A; AB/CB=7-241.
DR PDB; 4V9K; X-ray; 3.50 A; AB/CB=7-241.
DR PDB; 4V9L; X-ray; 3.50 A; AB/CB=7-241.
DR PDB; 4V9M; X-ray; 4.00 A; AB/CB=7-241.
DR PDB; 4V9N; X-ray; 3.40 A; AB/CB=7-240.
DR PDB; 4V9Q; X-ray; 3.40 A; BB/DB=7-240.
DR PDB; 4W29; X-ray; 3.80 A; AB/CB=7-241.
DR PDB; 4XEJ; X-ray; 3.80 A; AS02/BS02=7-240.
DR PDB; 5J4D; X-ray; 3.10 A; KA/PC=1-256.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4G; -.
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; P62662; -.
DR SMR; P62662; -.
DR IntAct; P62662; 4.
DR STRING; 262724.TT_C0509; -.
DR DrugBank; DB08185; 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DR EnsemblBacteria; AAS80857; AAS80857; TT_C0509.
DR GeneID; 3170121; -.
DR KEGG; tth:TT_C0509; -.
DR eggNOG; COG0052; Bacteria.
DR HOGENOM; CLU_040318_1_2_0; -.
DR OMA; SYIDRAY; -.
DR OrthoDB; 1623045at2; -.
DR EvolutionaryTrace; P62662; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR12534; PTHR12534; 1.
DR Pfam; PF00318; Ribosomal_S2; 1.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01011; rpsB_bact; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..256
FT /note="30S ribosomal protein S2"
FT /id="PRO_0000134263"
FT COILED 104..149
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:4V84"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 150..154
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 256 AA; 29277 MW; 65D7958336911CE5 CRC64;
MPVEITVKEL LEAGVHFGHE RKRWNPKFAR YIYAERNGIH IIDLQKTMEE LERTFRFIED
LAMRGGTILF VGTKKQAQDI VRMEAERAGM PYVNQRWLGG MLTNFKTISQ RVHRLEELEA
LFASPEIEER PKKEQVRLKH ELERLQKYLS GFRLLKRLPD AIFVVDPTKE AIAVREARKL
FIPVIALADT DSDPDLVDYI IPGNDDAIRS IQLILSRAVD LIIQARGGVV EPSPSYALVQ
EAEATETPEG ESEVEA
