RS14_BACSU
ID RS14_BACSU Reviewed; 61 AA.
AC P12878;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=30S ribosomal protein S14;
DE AltName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364};
DE AltName: Full=30S ribosomal protein S14-1;
DE AltName: Full=BS-A;
GN Name=rpsN1;
GN Synonyms=rpsN {ECO:0000255|HAMAP-Rule:MF_01364},
GN rpsNA {ECO:0000255|HAMAP-Rule:MF_01364}, rpsZ; OrderedLocusNames=BSU01290;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2508062; DOI=10.1093/nar/17.18.7469;
RA Henkin T.M., Moon S.H., Mattheakis L.C., Nomura M.;
RT "Cloning and analysis of the spc ribosomal protein operon of Bacillus
RT subtilis: comparison with the spc operon of Escherichia coli.";
RL Nucleic Acids Res. 17:7469-7486(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT alpha region.";
RL Gene 169:17-23(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 2-22.
RX PubMed=6806564; DOI=10.1007/bf00330792;
RA Higo K., Otaka E., Osawa S.;
RT "Purification and characterization of 30S ribosomal proteins from Bacillus
RT subtilis: correlation to Escherichia coli 30S proteins.";
RL Mol. Gen. Genet. 185:239-244(1982).
RN [5]
RP DISRUPTION PHENOTYPE, AND IDENTIFICATION IN RIBOSOME COMPLEX.
RC STRAIN=168;
RX PubMed=17163968; DOI=10.1111/j.1365-2958.2006.05513.x;
RA Natori Y., Nanamiya H., Akanuma G., Kosono S., Kudo T., Ochi K.,
RA Kawamura F.;
RT "A fail-safe system for the ribosome under zinc-limiting conditions in
RT Bacillus subtilis.";
RL Mol. Microbiol. 63:294-307(2007).
RN [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-61 WITH AND WITHOUT
RP VIRGINIAMYCIN M, AND SUBUNIT.
RX PubMed=30126986; DOI=10.1073/pnas.1808535115;
RA Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M.,
RA Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.;
RT "Structural basis for antibiotic resistance mediated by the Bacillus
RT subtilis ABCF ATPase VmlR.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018).
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 (By similarity). The major S14 protein in the
CC ribosome. Required for binding of S2 and S3 to the 30S subunit and for
CC association of the 30S with the 50S subunit. {ECO:0000255|HAMAP-
CC 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 (PubMed:30126986,
CC PubMed:17163968). Contacts proteins S3 and S10 (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01364, ECO:0000269|PubMed:17163968,
CC ECO:0000269|PubMed:30126986}.
CC -!- DISRUPTION PHENOTYPE: Cannot be disrupted; as the protein decreases in
CC cells 70S ribosome formation decreases rapidly, with concomitant loss
CC of S2, S3 and YugI proteins from the 30S subunit.
CC {ECO:0000269|PubMed:17163968}.
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; X15664; CAA33704.1; -; Genomic_DNA.
DR EMBL; L47971; AAB06812.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11905.1; -; Genomic_DNA.
DR PIR; S05995; R3BS14.
DR RefSeq; NP_388010.1; NC_000964.3.
DR RefSeq; WP_003156488.1; NZ_JNCM01000029.1.
DR PDB; 3J9W; EM; 3.90 A; AN=1-61.
DR PDB; 5NJT; EM; 3.80 A; N=2-61.
DR PDB; 6HA1; EM; 3.10 A; n=1-61.
DR PDB; 6HA8; EM; 3.50 A; n=1-61.
DR PDB; 6HTQ; EM; 4.50 A; n=2-61.
DR PDB; 7O5B; EM; 3.33 A; N=1-61.
DR PDB; 7QV1; EM; 3.50 A; n=1-61.
DR PDB; 7QV2; EM; 3.50 A; n=1-61.
DR PDB; 7QV3; EM; 5.14 A; n=1-61.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P12878; -.
DR SMR; P12878; -.
DR STRING; 224308.BSU01290; -.
DR PaxDb; P12878; -.
DR EnsemblBacteria; CAB11905; CAB11905; BSU_01290.
DR GeneID; 64301967; -.
DR GeneID; 66328076; -.
DR GeneID; 935946; -.
DR KEGG; bsu:BSU01290; -.
DR PATRIC; fig|224308.179.peg.132; -.
DR eggNOG; COG0199; Bacteria.
DR InParanoid; P12878; -.
DR OMA; RAYTRCN; -.
DR PhylomeDB; P12878; -.
DR BioCyc; BSUB:BSU01290-MON; -.
DR PRO; PR:P12878; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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; Direct protein sequencing; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6806564"
FT CHAIN 2..61
FT /note="30S ribosomal protein S14"
FT /id="PRO_0000130872"
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; 7246 MW; FC37E9953A148F35 CRC64;
MAKKSMIAKQ QRTPKFKVQE YTRCERCGRP HSVIRKFKLC RICFRELAYK GQIPGVKKAS
W
