ZITR_LACLM
ID ZITR_LACLM Reviewed; 145 AA.
AC A2RNS2;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Transcriptional regulator ZitR;
GN Name=zitR; OrderedLocusNames=llmg_2401;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=MG1363;
RX PubMed=21317326; DOI=10.1128/jb.01109-10;
RA Llull D., Son O., Blanie S., Briffotaux J., Morello E., Rogniaux H.,
RA Danot O., Poquet I.;
RT "Lactococcus lactis ZitR is a zinc-responsive repressor active in the
RT presence of low, nontoxic zinc concentrations in vivo.";
RL J. Bacteriol. 193:1919-1929(2011).
CC -!- FUNCTION: Zinc-responsive regulator that represses expression of the
CC zit operon in the presence of zinc. Acts by binding two palindromic
CC operator sites overlapping the -35 and -10 boxes of the zit promoter.
CC Could be a sensitive sensor of intracellular zinc to efficiently
CC respond to zinc variations in the environment.
CC {ECO:0000269|PubMed:21317326}.
CC -!- ACTIVITY REGULATION: Zinc acts as a corepressor and is required for
CC DNA-binding activity. Binds up to two zinc ligands per monomer.
CC Inactive under zinc deprivation. {ECO:0000269|PubMed:21317326}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21317326}.
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DR EMBL; AM406671; CAL98965.1; -; Genomic_DNA.
DR RefSeq; WP_011836041.1; NZ_WJVF01000024.1.
DR PDB; 6FI9; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-145.
DR PDBsum; 6FI9; -.
DR AlphaFoldDB; A2RNS2; -.
DR SMR; A2RNS2; -.
DR STRING; 416870.llmg_2401; -.
DR EnsemblBacteria; CAL98965; CAL98965; llmg_2401.
DR GeneID; 61110444; -.
DR KEGG; llm:llmg_2401; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_142321_1_0_9; -.
DR OMA; INATQAH; -.
DR PhylomeDB; A2RNS2; -.
DR BioCyc; LLAC416870:LLMG_RS12040-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..145
FT /note="Transcriptional regulator ZitR"
FT /id="PRO_0000425608"
FT DOMAIN 1..142
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT DNA_BIND 53..76
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:6FI9"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6FI9"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6FI9"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 101..123
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:6FI9"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6FI9"
SQ SEQUENCE 145 AA; 16334 MW; 55A6837568046124 CRC64;
MSLANQIDQF LGAIMQFAEN KHEILLGECE SNVKLTSTQE HILMILAAEV STNARIAEQL
KISPAAVTKA LKKLQEQELI KSSRATNDER VVLWSLTEKA IPVAKEHAAH HEKTLSTYQE
LGDKFTDEEQ KVISQFLSVL TEEFR
