ZUR_MYCTU
ID ZUR_MYCTU Reviewed; 130 AA.
AC P9WN85; F2GIN3; L0TC35; O05839; Q7D799;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Zinc uptake regulation protein;
DE Short=Zinc uptake regulator;
GN Name=zur; Synonyms=fur-2, furB; OrderedLocusNames=Rv2359;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION, COFACTOR, AND ZINC-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15059632; DOI=10.1016/j.resmic.2003.11.009;
RA Milano A., Branzoni M., Canneva F., Profumo A., Riccardi G.;
RT "The Mycobacterium tuberculosis Rv2358-furB operon is induced by zinc.";
RL Res. Microbiol. 155:192-200(2004).
RN [3]
RP INDUCTION.
RX PubMed=16077132; DOI=10.1128/jb.187.16.5837-5840.2005;
RA Canneva F., Branzoni M., Riccardi G., Provvedi R., Milano A.;
RT "Rv2358 and FurB: two transcriptional regulators from Mycobacterium
RT tuberculosis which respond to zinc.";
RL J. Bacteriol. 187:5837-5840(2005).
RN [4]
RP FUNCTION, DNA-BINDING, COFACTOR, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17098899; DOI=10.1128/jb.01190-06;
RA Maciag A., Dainese E., Rodriguez G.M., Milano A., Provvedi R., Pasca M.R.,
RA Smith I., Palu G., Riccardi G., Manganelli R.;
RT "Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon.";
RL J. Bacteriol. 189:730-740(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-130 IN COMPLEX WITH ZINC,
RP COFACTOR, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17213192; DOI=10.1074/jbc.m609974200;
RA Lucarelli D., Russo S., Garman E., Milano A., Meyer-Klaucke W., Pohl E.;
RT "Crystal structure and function of the zinc uptake regulator FurB from
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 282:9914-9922(2007).
CC -!- FUNCTION: Global transcriptional regulator involved in zinc
CC homeostasis. Represses the transcription of at least 32 genes,
CC including genes involved in zinc homeostasis, by binding to promoter
CC sequences that contain a conserved 26 bp palindrome, in the presence of
CC zinc. {ECO:0000269|PubMed:17098899}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15059632, ECO:0000269|PubMed:17098899,
CC ECO:0000269|PubMed:17213192};
CC Note=Binds 2 Zn(2+) ions per subunit. Three distinct zinc binding-sites
CC were identified in the crystal structure, but the exact biological
CC function of the third site remains to be determined. It could be an
CC artifact of crystallization. {ECO:0000269|PubMed:15059632,
CC ECO:0000269|PubMed:17098899, ECO:0000269|PubMed:17213192};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17213192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Induced by zinc. Repressed by SmtB in the absence of zinc.
CC {ECO:0000269|PubMed:15059632, ECO:0000269|PubMed:16077132}.
CC -!- DOMAIN: The N-terminal domain binds DNA and the C-terminal domain is
CC involved in metal-binding and dimerization.
CC {ECO:0000269|PubMed:17213192}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45147.1; -; Genomic_DNA.
DR PIR; F70585; F70585.
DR RefSeq; NP_216875.1; NC_000962.3.
DR RefSeq; WP_003899290.1; NZ_NVQJ01000029.1.
DR PDB; 2O03; X-ray; 2.70 A; A=2-130.
DR PDBsum; 2O03; -.
DR AlphaFoldDB; P9WN85; -.
DR SMR; P9WN85; -.
DR STRING; 83332.Rv2359; -.
DR PaxDb; P9WN85; -.
DR DNASU; 886009; -.
DR GeneID; 886009; -.
DR KEGG; mtu:Rv2359; -.
DR TubercuList; Rv2359; -.
DR eggNOG; COG0735; Bacteria.
DR OMA; HDHVILT; -.
DR PhylomeDB; P9WN85; -.
DR Proteomes; UP000001584; Chromosome.
DR CollecTF; EXPREG_00000c60; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; EXP:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0010043; P:response to zinc ion; IGI:MTBBASE.
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 3D-structure; Cytoplasm; DNA-binding; Metal-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..130
FT /note="Zinc uptake regulation protein"
FT /id="PRO_0000419204"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:17213192"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:17213192"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:2O03"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:2O03"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:2O03"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:2O03"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2O03"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2O03"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:2O03"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2O03"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2O03"
SQ SEQUENCE 130 AA; 14398 MW; 0C826782ED586F13 CRC64;
MSAAGVRSTR QRAAISTLLE TLDDFRSAQE LHDELRRRGE NIGLTTVYRT LQSMASSGLV
DTLHTDTGES VYRRCSEHHH HHLVCRSCGS TIEVGDHEVE AWAAEVATKH GFSDVSHTIE
IFGTCSDCRS
