(data stored in SCRATCH zone)

SWISSPROT: ZUR_BACSU

ID   ZUR_BACSU               Reviewed;         145 AA.
AC   P54479;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 114.
DE   RecName: Full=Zinc-specific metallo-regulatory protein;
GN   Name=zur; Synonyms=yqfV; OrderedLocusNames=BSU25100;
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 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
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   SEQUENCE REVISION TO 12.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   CHARACTERIZATION, AND FUNCTION.
RX   PubMed=9811636;
RA   Gaballa A., Helmann J.D.;
RT   "Identification of a zinc-specific metalloregulatory protein, Zur,
RT   controlling zinc transport operons in Bacillus subtilis.";
RL   J. Bacteriol. 180:5815-5821(1998).
RN   [5]
RP   FUNCTION IN REPRESSION OF EXPRESSION OF RIBOSOMAL PROTEIN RL31B.
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   [6]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, DOMAIN, ZINC-BINDING,
RP   AND MUTAGENESIS OF GLU-70; CYS-84; HIS-89; HIS-90; HIS-91; HIS-92; CYS-95;
RP   CYS-98; ASP-110; HIS-124; CYS-132 AND CYS-135.
RX   PubMed=21821657; DOI=10.1093/nar/gkr625;
RA   Ma Z., Gabriel S.E., Helmann J.D.;
RT   "Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur.";
RL   Nucleic Acids Res. 39:9130-9138(2011).
CC   -!- FUNCTION: Acts as a negative controlling element, employing Zn(2+) as a
CC       cofactor to bind the operator of the repressed genes. Required for the
CC       zinc-specific repression of two operons implicated in zinc uptake, yciC
CC       and ycdHIyceA. Also represses the expression of rpmE2, the gene for
CC       ribosomal protein L31B, which is expressed only after the end of
CC       exponential growth. {ECO:0000269|PubMed:15049826,
CC       ECO:0000269|PubMed:21821657, ECO:0000269|PubMed:9811636}.
CC   -!- ACTIVITY REGULATION: Sequentially activated from an inactive dimer
CC       (Zur(2):Zn(2)) to a partially active asymmetric dimer (Zur(2):Zn(3)),
CC       and finally to the fully zinc-loaded active form (Zur(2):Zn(4)). Binds
CC       a maximum of 4 Zn(2+) ions per dimer. {ECO:0000269|PubMed:21821657}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21821657}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Contains 3 zinc-binding sites. Site 1 has a structural role and
CC       site 2 is the Zn(2+) sensing site. Site 3 residues do not bind metal
CC       ions with a physiologically relevant affinity, but contribute to dimer
CC       stability. {ECO:0000269|PubMed:21821657}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
DR   EMBL; D84432; BAA12499.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14440.2; -; Genomic_DNA.
DR   PIR; H69954; H69954.
DR   RefSeq; NP_390389.2; NC_000964.3.
DR   RefSeq; WP_004398578.1; NZ_JNCM01000036.1.
DR   SMR; P54479; -.
DR   STRING; 224308.BSU25100; -.
DR   PaxDb; P54479; -.
DR   PRIDE; P54479; -.
DR   EnsemblBacteria; CAB14440; CAB14440; BSU25100.
DR   GeneID; 937968; -.
DR   KEGG; bsu:BSU25100; -.
DR   PATRIC; fig|224308.179.peg.2729; -.
DR   eggNOG; ENOG4105N80; Bacteria.
DR   eggNOG; COG0735; LUCA.
DR   HOGENOM; HOG000014143; -.
DR   InParanoid; P54479; -.
DR   KO; K02076; -.
DR   OMA; FEIYGTC; -.
DR   PhylomeDB; P54479; -.
DR   BioCyc; BSUB:BSU25100-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   CollecTF; EXPREG_00000b30; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:CollecTF.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:CollecTF.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR   GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR   CDD; cd07153; Fur_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR002481; FUR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR33202; PTHR33202; 1.
DR   Pfam; PF01475; FUR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54479.
DR   SWISS-2DPAGE; P54479.
KW   Cytoplasm; DNA-binding; Metal-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..145
FT                   /note="Zinc-specific metallo-regulatory protein"
FT                   /id="PRO_0000095591"
FT   COMPBIAS        88..92
FT                   /note="His-rich"
FT   MUTAGEN         70
FT                   /note="E->A: Does not affect repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         84
FT                   /note="C->S: Decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         89
FT                   /note="H->A: Decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         90
FT                   /note="H->A: Decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         91
FT                   /note="H->A: Decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         92
FT                   /note="H->A: Decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         95
FT                   /note="C->S: Lack of repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         98
FT                   /note="C->S: Lack of repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         110
FT                   /note="D->A: Does not affect repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         124
FT                   /note="H->A: Strong decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         132
FT                   /note="C->S: Strong decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   MUTAGEN         135
FT                   /note="C->S: Strong decrease in repressor activity."
FT                   /evidence="ECO:0000269|PubMed:21821657"
FT   CONFLICT        12
FT                   /note="E -> G (in Ref. 1; BAA12499)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   145 AA;  16637 MW;  484AF8DCA4AFC396 CRC64;
     MNVQEALNLL KENGYKYTNK REDMLQLFAD SDRYLTAKNV LSALNDDYPG LSFDTIYRNL
     SLYEELGILE TTELSGEKLF RFKCSFTHHH HHFICLACGK TKEIESCPMD KLCDDLDGYQ
     VSGHKFEIYG TCPDCTAENQ ENTTA
//

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