RL332_BACSU
ID RL332_BACSU Reviewed; 49 AA.
AC Q06798;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L33 2;
GN Name=rpmGB; Synonyms=rpmG, rpmG2; OrderedLocusNames=BSU00990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7968510; DOI=10.1111/j.1365-2958.1993.tb00910.x;
RA Jeong S., Yoshikawa H., Takahashi H.;
RT "Isolation and characterization of the secE homologue gene of Bacillus
RT subtilis.";
RL Mol. Microbiol. 10:133-142(1993).
RN [2]
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 [3]
RP THIOSTREPTON RESISTANCE.
RX PubMed=6248722; DOI=10.1007/bf00270472;
RA Smith I., Paress P., Cabane K., Dubnau E.;
RT "Genetics and physiology of the rel system of Bacillus subtilis.";
RL Mol. Gen. Genet. 178:271-279(1980).
RN [4]
RP DISRUPTION PHENOTYPE, AND ROLE IN SPORULATION.
RC STRAIN=168;
RX PubMed=14586115; DOI=10.1271/bbb.67.2245;
RA Ohashi Y., Inaoka T., Kasai K., Ito Y., Okamoto S., Satsu H., Tozawa Y.,
RA Kawamura F., Ochi K.;
RT "Expression profiling of translation-associated genes in sporulating
RT Bacillus subtilis and consequence of sporulation by gene inactivation.";
RL Biosci. Biotechnol. Biochem. 67:2245-2253(2003).
CC -!- FUNCTION: Plays a role in sporulation at high temperatures.
CC {ECO:0000269|PubMed:14586115}.
CC -!- DISRUPTION PHENOTYPE: No effect on sporulation at 37 degrees Celsius,
CC however sporulation decreases at 47 degrees Celsius.
CC {ECO:0000269|PubMed:14586115}.
CC -!- MISCELLANEOUS: An unknown mutation in this protein gives rise to
CC thiostrepton resistance.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family.
CC {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; D13303; BAA02558.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11875.1; -; Genomic_DNA.
DR PIR; S39857; S39857.
DR RefSeq; NP_387980.1; NC_000964.3.
DR RefSeq; WP_003156421.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; Q06798; -.
DR SMR; Q06798; -.
DR STRING; 224308.BSU00990; -.
DR PaxDb; Q06798; -.
DR PRIDE; Q06798; -.
DR EnsemblBacteria; CAB11875; CAB11875; BSU_00990.
DR GeneID; 64301937; -.
DR GeneID; 66327880; -.
DR GeneID; 936842; -.
DR KEGG; bsu:BSU00990; -.
DR PATRIC; fig|224308.179.peg.102; -.
DR eggNOG; COG0267; Bacteria.
DR InParanoid; Q06798; -.
DR PhylomeDB; Q06798; -.
DR BioCyc; BSUB:BSU00990-MON; -.
DR PRO; PR:Q06798; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.20.28.120; -; 1.
DR HAMAP; MF_00294; Ribosomal_L33; 1.
DR InterPro; IPR038584; L33_sf.
DR InterPro; IPR001705; Ribosomal_L33.
DR InterPro; IPR018264; Ribosomal_L33_CS.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR43168; PTHR43168; 1.
DR Pfam; PF00471; Ribosomal_L33; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR TIGRFAMs; TIGR01023; rpmG_bact; 1.
DR PROSITE; PS00582; RIBOSOMAL_L33; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..49
FT /note="50S ribosomal protein L33 2"
FT /id="PRO_0000170140"
SQ SEQUENCE 49 AA; 5496 MW; 3D91426D93C11ED4 CRC64;
MRKKITLACK TCGNRNYTTM KSSASAAERL EVKKYCSTCN SHTAHLETK
