ID   YACG_LEGPL              Reviewed;          70 AA.
AC   Q5WZW1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; OrderedLocusNames=lpl0270;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Inhibits all the catalytic activities of DNA gyrase by
CC       preventing its interaction with DNA. Acts by binding directly to the C-
CC       terminal domain of GyrB, which probably disrupts DNA binding by the
CC       gyrase. {ECO:0000255|HAMAP-Rule:MF_00649}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00649};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00649};
CC   -!- SUBUNIT: Interacts with GyrB. {ECO:0000255|HAMAP-Rule:MF_00649}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family.
CC       {ECO:0000255|HAMAP-Rule:MF_00649}.
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DR   EMBL; CR628337; CAH14501.1; -; Genomic_DNA.
DR   RefSeq; WP_011214535.1; NC_006369.1.
DR   AlphaFoldDB; Q5WZW1; -.
DR   SMR; Q5WZW1; -.
DR   EnsemblBacteria; CAH14501; CAH14501; lpl0270.
DR   KEGG; lpf:lpl0270; -.
DR   LegioList; lpl0270; -.
DR   HOGENOM; CLU_178280_1_0_6; -.
DR   OMA; WAAEEHK; -.
DR   Proteomes; UP000002517; Chromosome.
DR   GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.30.50.10; -; 1.
DR   HAMAP; MF_00649; DNA_gyrase_inhibitor_YacG; 1.
DR   InterPro; IPR005584; DNA_gyrase_inhibitor_YacG.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR36150; PTHR36150; 1.
DR   Pfam; PF03884; YacG; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Zinc.
FT   CHAIN           1..70
FT                   /note="DNA gyrase inhibitor YacG"
FT                   /id="PRO_0000211705"
FT   REGION          43..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
SQ   SEQUENCE   70 AA;  8054 MW;  05502F7E529C1A67 CRC64;
     MNNQQKIKCP ICGKQNTWRP DNQFRPFCSE RCKLIDLGEW ASESRKIPGS SIDPESIVTS
     NNKQDNVDEQ