RL31_BACSU
ID RL31_BACSU Reviewed; 66 AA.
AC Q03223;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=50S ribosomal protein L31;
GN Name=rpmE; OrderedLocusNames=BSU37070;
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=BD99 / MS119;
RX PubMed=8423140; DOI=10.1128/jb.175.3.647-654.1993;
RA Quirk P.G., Dunkley E.A. Jr., Lee P., Krulwich T.A.;
RT "Identification of a putative Bacillus subtilis rho gene.";
RL J. Bacteriol. 175:647-654(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 CHARACTERIZATION OF GROWTH-PHASE DEPENDENT EXPRESSION, COFACTOR, AND
RP MUTAGENESIS OF CYS-36 AND CYS-39.
RC STRAIN=168;
RX PubMed=15049826; DOI=10.1111/j.1365-2958.2003.03972.x;
RA Nanamiya H., Akanuma G., Natori Y., Murayama R., Kosono S., Kudo T.,
RA Kobayashi K., Ogasawara N., Park S.-M., Ochi K., Kawamura F.;
RT "Zinc is a key factor in controlling alternation of two types of L31
RT protein in the Bacillus subtilis ribosome.";
RL Mol. Microbiol. 52:273-283(2004).
RN [5]
RP ALTERNATION OF L31 PARALOGS IN THE RIBOSOME.
RX PubMed=16547061; DOI=10.1128/jb.188.7.2715-2720.2006;
RA Akanuma G., Nanamiya H., Natori Y., Nomura N., Kawamura F.;
RT "Liberation of zinc-containing L31 (rpmE) from ribosomes by its paralogous
RT gene product, ytiA, in Bacillus subtilis.";
RL J. Bacteriol. 188:2715-2720(2006).
RN [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-66 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 the 23S rRNA. {ECO:0000250}.
CC -!- FUNCTION: While neither of the L31 paralogs is essential, this protein
CC seems to function as the main L31 protein. Has a lower affinity for 70S
CC ribosomes than the non-zinc-containing paralog L31B (ytiA); is
CC displaced by it to varying extents, even under zinc-replete conditions.
CC {ECO:0000269|PubMed:16547061}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15049826};
CC Note=Binds 1 zinc ion per subunit. This zinc stabilizes the protein.
CC {ECO:0000269|PubMed:15049826};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit during exponential growth.
CC {ECO:0000269|PubMed:15049826, ECO:0000269|PubMed:30126986}.
CC -!- INDUCTION: Only accumulates during exponential growth.
CC {ECO:0000269|PubMed:15049826}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC Type A subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M97678; AAA02901.1; -; Unassigned_DNA.
DR EMBL; Z49782; CAA89878.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15724.1; -; Genomic_DNA.
DR PIR; S55431; S55431.
DR RefSeq; NP_391588.1; NC_000964.3.
DR RefSeq; WP_003151132.1; NZ_JNCM01000034.1.
DR PDB; 3J9W; EM; 3.90 A; B3=1-66.
DR PDB; 5NJT; EM; 3.80 A; y=1-64.
DR PDB; 6HA1; EM; 3.10 A; 6=1-63.
DR PDB; 6HA8; EM; 3.50 A; 6=1-66.
DR PDB; 6HTQ; EM; 4.50 A; Z=1-63.
DR PDB; 7O5B; EM; 3.33 A; 6=1-66.
DR PDB; 7QV1; EM; 3.50 A; 6=1-66.
DR PDB; 7QV2; EM; 3.50 A; 6=1-66.
DR PDB; 7QV3; EM; 5.14 A; 6=1-66.
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; Q03223; -.
DR SMR; Q03223; -.
DR STRING; 224308.BSU37070; -.
DR jPOST; Q03223; -.
DR PaxDb; Q03223; -.
DR PRIDE; Q03223; -.
DR EnsemblBacteria; CAB15724; CAB15724; BSU_37070.
DR GeneID; 64305482; -.
DR GeneID; 66324594; -.
DR GeneID; 937034; -.
DR KEGG; bsu:BSU37070; -.
DR PATRIC; fig|224308.179.peg.4015; -.
DR eggNOG; COG0254; Bacteria.
DR InParanoid; Q03223; -.
DR OMA; WYPDAKV; -.
DR PhylomeDB; Q03223; -.
DR BioCyc; BSUB:BSU37070-MON; -.
DR PRO; PR:Q03223; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 4.10.830.30; -; 1.
DR HAMAP; MF_00501; Ribosomal_L31_1; 1.
DR InterPro; IPR034704; L28p-like.
DR InterPro; IPR002150; Ribosomal_L31.
DR InterPro; IPR027491; Ribosomal_L31_A.
DR InterPro; IPR042105; Ribosomal_L31_sf.
DR PANTHER; PTHR33280; PTHR33280; 1.
DR Pfam; PF01197; Ribosomal_L31; 1.
DR PRINTS; PR01249; RIBOSOMALL31.
DR SUPFAM; SSF143800; SSF143800; 1.
DR TIGRFAMs; TIGR00105; L31; 1.
DR PROSITE; PS01143; RIBOSOMAL_L31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..66
FT /note="50S ribosomal protein L31"
FT /id="PRO_0000173079"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 36
FT /note="C->A: The protein does not accumulate and cells grow
FT very slowly."
FT /evidence="ECO:0000269|PubMed:15049826"
FT MUTAGEN 39
FT /note="C->A: The protein does not accumulate and cells grow
FT very slowly."
FT /evidence="ECO:0000269|PubMed:15049826"
SQ SEQUENCE 66 AA; 7444 MW; 02EFB5B4A02CA46D CRC64;
MKAGIHPNFK KATVKCACGN EFETGSVKEE VRVEICSECH PFYTGRQKFA SADGRVDRFN
KKYGLK
