RS14Z_HERA2
ID RS14Z_HERA2 Reviewed; 61 AA.
AC A9B424;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Haur_4927;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000875; ABX07557.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B424; -.
DR SMR; A9B424; -.
DR STRING; 316274.Haur_4927; -.
DR EnsemblBacteria; ABX07557; ABX07557; Haur_4927.
DR KEGG; hau:Haur_4927; -.
DR eggNOG; COG0199; Bacteria.
DR HOGENOM; CLU_139869_3_0_0; -.
DR OMA; RAYTRCN; -.
DR Proteomes; UP000000787; 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; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..61
FT /note="30S ribosomal protein S14 type Z"
FT /id="PRO_1000143909"
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; 6985 MW; 5357BF68B239BF63 CRC64;
MAKKSMIVKA NRAPKFSTQG YNRCKRCGRP RAYMRKFGIC RICFRELASQ GLIPGVTKSS
W