(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 113.
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}.
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   SMR; Q06798; -.
DR   STRING; 224308.BSU00990; -.
DR   PaxDb; Q06798; -.
DR   PRIDE; Q06798; -.
DR   EnsemblBacteria; CAB11875; CAB11875; BSU00990.
DR   GeneID; 936842; -.
DR   GeneID; 9780089; -.
DR   KEGG; bsu:BSU00990; -.
DR   PATRIC; fig|224308.179.peg.102; -.
DR   eggNOG; COG0267; LUCA.
DR   HOGENOM; HOG000004838; -.
DR   InParanoid; Q06798; -.
DR   KO; K02913; -.
DR   PhylomeDB; Q06798; -.
DR   BioCyc; BSUB:BSU00990-MONOMER; -.
DR   PRO; PR:Q06798; -.
DR   Proteomes; UP000001570; Chromosome.
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   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;
DR   PRODOM; Q06798.
DR   SWISS-2DPAGE; Q06798.
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
//

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