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RS14Z_STRE4
ID   RS14Z_STRE4             Reviewed;          61 AA.
AC   C0M9Z1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=rpsN {ECO:0000255|HAMAP-Rule:MF_01364};
GN   OrderedLocusNames=SEQ_0068;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW91991.1; -; Genomic_DNA.
DR   RefSeq; WP_012514742.1; NC_012471.1.
DR   AlphaFoldDB; C0M9Z1; -.
DR   SMR; C0M9Z1; -.
DR   EnsemblBacteria; CAW91991; CAW91991; SEQ_0068.
DR   GeneID; 64010214; -.
DR   KEGG; seu:SEQ_0068; -.
DR   HOGENOM; CLU_139869_3_0_9; -.
DR   OMA; RAYTRCN; -.
DR   Proteomes; UP000001365; 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   3: Inferred from homology;
KW   Metal-binding; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Zinc.
FT   CHAIN           1..61
FT                   /note="30S ribosomal protein S14 type Z"
FT                   /id="PRO_1000166780"
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"
SQ   SEQUENCE   61 AA;  7099 MW;  51947B92FD5C05AB CRC64;
     MAKKSMIAKN KRPAKYSTQA YTRCEKCGRP HSVYRKFKLC RVCFRELAYK GQIPGVVKAS
     W
 
 
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