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 03-AUG-2022, entry version 126.
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; DOI=10.1128/jb.180.22.5815-5821.1998;
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}.
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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 AlphaFoldDB; P54479; -.
DR SMR; P54479; -.
DR STRING; 224308.BSU25100; -.
DR jPOST; P54479; -.
DR PaxDb; P54479; -.
DR PRIDE; P54479; -.
DR EnsemblBacteria; CAB14440; CAB14440; BSU_25100.
DR GeneID; 937968; -.
DR KEGG; bsu:BSU25100; -.
DR PATRIC; fig|224308.179.peg.2729; -.
DR eggNOG; COG0735; Bacteria.
DR InParanoid; P54479; -.
DR OMA; FEIYGTC; -.
DR PhylomeDB; P54479; -.
DR BioCyc; BSUB:BSU25100-MON; -.
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; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP: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 Gene3D; 3.30.1490.190; -; 1.
DR InterPro; IPR002481; FUR.
DR InterPro; IPR043135; Fur_C.
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;
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 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
