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RS14Z_THET2
ID   RS14Z_THET2             Reviewed;          61 AA.
AC   P62656;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364};
GN   Name=rpsZ {ECO:0000255|HAMAP-Rule:MF_01364};
GN   Synonyms=rps14 {ECO:0000255|HAMAP-Rule:MF_01364},
GN   rpsN {ECO:0000255|HAMAP-Rule:MF_01364}; OrderedLocusNames=TT_C1315;
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: Binds 16S rRNA, required for the assembly of 30S particles
CC       and may also be responsible for determining the conformation of the 16S
CC       rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01364};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01364};
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 and
CC       S10. {ECO:0000255|HAMAP-Rule:MF_01364}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC       Zinc-binding uS14 subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}.
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DR   EMBL; AE017221; AAS81657.1; -; Genomic_DNA.
DR   RefSeq; WP_008633399.1; NC_005835.1.
DR   PDB; 4KVB; X-ray; 4.20 A; N=1-61.
DR   PDB; 4V4J; X-ray; 3.83 A; o=1-61.
DR   PDB; 4V63; X-ray; 3.21 A; AN/CN=1-61.
DR   PDB; 4V67; X-ray; 3.00 A; AN/CN=1-61.
DR   PDB; 4V7P; X-ray; 3.62 A; AN/DN=2-61.
DR   PDB; 4V83; X-ray; 3.50 A; AN/CN=2-61.
DR   PDB; 4V84; X-ray; 3.40 A; AN/CN=2-61.
DR   PDB; 4V9J; X-ray; 3.86 A; AN/CN=2-61.
DR   PDB; 4V9K; X-ray; 3.50 A; AN/CN=2-61.
DR   PDB; 4V9L; X-ray; 3.50 A; AN/CN=2-61.
DR   PDB; 4V9M; X-ray; 4.00 A; AN/CN=2-61.
DR   PDB; 4V9N; X-ray; 3.40 A; AN/CN=2-61.
DR   PDB; 4V9Q; X-ray; 3.40 A; BN/DN=2-61.
DR   PDB; 4W29; X-ray; 3.80 A; AN/CN=2-61.
DR   PDB; 4XEJ; X-ray; 3.80 A; AS14/BS14=2-61.
DR   PDB; 5J4D; X-ray; 3.10 A; BD/WA=1-61.
DR   PDBsum; 4KVB; -.
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; P62656; -.
DR   SMR; P62656; -.
DR   IntAct; P62656; 4.
DR   STRING; 262724.TT_C1315; -.
DR   EnsemblBacteria; AAS81657; AAS81657; TT_C1315.
DR   GeneID; 3169802; -.
DR   KEGG; tth:TT_C1315; -.
DR   eggNOG; COG0199; Bacteria.
DR   HOGENOM; CLU_139869_3_0_0; -.
DR   OMA; RAYTRCN; -.
DR   OrthoDB; 2032609at2; -.
DR   EvolutionaryTrace; P62656; -.
DR   Proteomes; UP000000592; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.830.10; -; 1.
DR   HAMAP; MF_01364_B; Ribosomal_S14_2_B; 1.
DR   InterPro; IPR001209; Ribosomal_S14.
DR   InterPro; IPR043140; Ribosomal_S14/S29.
DR   InterPro; IPR018271; Ribosomal_S14_CS.
DR   InterPro; IPR023053; Ribosomal_S14_Z.
DR   PANTHER; PTHR19836; PTHR19836; 1.
DR   Pfam; PF00253; Ribosomal_S14; 1.
DR   PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..61
FT                   /note="30S ribosomal protein S14 type Z"
FT                   /id="PRO_0000130954"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01364"
FT   HELIX           4..12
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            35..38
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:4V63"
SQ   SEQUENCE   61 AA;  7140 MW;  BEE8AB1E1E86B531 CRC64;
     MARKALIEKA KRTPKFKVRA YTRCVRCGRA RSVYRFFGLC RICLRELAHK GQLPGVRKAS
     W
 
 
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