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Database: UniProt
Entry: L0ET18_LIBCB
LinkDB: L0ET18_LIBCB
Original site: L0ET18_LIBCB 
ID   L0ET18_LIBCB            Unreviewed;        63 AA.
AC   L0ET18;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   OrderedLocusNames=B488_00890 {ECO:0000313|EMBL:AGA64082.1};
OS   Liberibacter crescens (strain BT-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64082.1, ECO:0000313|Proteomes:UP000010799};
RN   [1] {ECO:0000313|EMBL:AGA64082.1, ECO:0000313|Proteomes:UP000010799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-1 {ECO:0000313|EMBL:AGA64082.1,
RC   ECO:0000313|Proteomes:UP000010799};
RX   PubMed=23408754; DOI=10.4056/sigs.3326772;
RA   Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT   "Complete genome sequence of Liberibacter crescens BT-1.";
RL   Stand. Genomic Sci. 7:271-283(2012).
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:0000256|HAMAP-Rule:MF_00649}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00649};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00649};
CC   -!- SUBUNIT: Interacts with GyrB. {ECO:0000256|HAMAP-Rule:MF_00649}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family.
CC       {ECO:0000256|HAMAP-Rule:MF_00649}.
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DR   EMBL; CP003789; AGA64082.1; -; Genomic_DNA.
DR   RefSeq; WP_015272509.1; NC_019907.1.
DR   AlphaFoldDB; L0ET18; -.
DR   STRING; 1215343.B488_00890; -.
DR   KEGG; lcc:B488_00890; -.
DR   PATRIC; fig|1215343.11.peg.94; -.
DR   eggNOG; COG3024; Bacteria.
DR   HOGENOM; CLU_178280_2_3_5; -.
DR   Proteomes; UP000010799; 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 DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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; DNA GYRASE INHIBITOR YACG; 1.
DR   PANTHER; PTHR36150:SF1; DNA GYRASE INHIBITOR YACG; 1.
DR   Pfam; PF03884; YacG; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00649}; Reference proteome {ECO:0000313|Proteomes:UP000010799};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ   SEQUENCE   63 AA;  7476 MW;  B528FCF0D7281C3C CRC64;
     MVELKRKIHP CPECKKMSEY KYYPFCSERC RLLDLSRWFS GDYIIKLSTH EGGVDEDCKD
     IAL
//
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