ID A0A0A1VIR9_9BURK Unreviewed; 73 AA.
AC A0A0A1VIR9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN ORFNames=AVS7_02927 {ECO:0000313|EMBL:GAD23167.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD23167.1};
RN [1] {ECO:0000313|EMBL:GAD23167.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD23167.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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; DF238937; GAD23167.1; -; Genomic_DNA.
DR RefSeq; WP_020229074.1; NZ_DF238937.1.
DR AlphaFoldDB; A0A0A1VIR9; -.
DR STRING; 1268622.AVS7_02927; -.
DR eggNOG; COG3024; Bacteria.
DR OrthoDB; 9809663at2; -.
DR Proteomes; UP000030646; Unassembled WGS sequence.
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:UP000030646};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ SEQUENCE 73 AA; 7972 MW; B76AA060BA04571D CRC64;
MATPAQQPSS SARQVPCPTC GGPSLYSPAN PYRPFCSERC RQIDLGAWAN EDFRMPAEAP
PEDAEYGDPK RLS
//
