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Database: UniProt
Entry: A0A1P8FQ94_9PROT
LinkDB: A0A1P8FQ94_9PROT
Original site: A0A1P8FQ94_9PROT 
ID   A0A1P8FQ94_9PROT        Unreviewed;        64 AA.
AC   A0A1P8FQ94;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   ORFNames=BWI17_03405 {ECO:0000313|EMBL:APV52268.1};
OS   Betaproteobacteria bacterium GR16-43.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV52268.1, ECO:0000313|Proteomes:UP000185830};
RN   [1] {ECO:0000313|EMBL:APV52268.1, ECO:0000313|Proteomes:UP000185830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GR16-43 {ECO:0000313|EMBL:APV52268.1,
RC   ECO:0000313|Proteomes:UP000185830};
RA   Choi A.;
RT   "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT   freshwater pond in South Korea.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; CP019169; APV52268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8FQ94; -.
DR   STRING; 1904640.BWI17_03405; -.
DR   KEGG; beba:BWI17_03405; -.
DR   OrthoDB; 9809663at2; -.
DR   Proteomes; UP000185830; 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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..64
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:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ   SEQUENCE   64 AA;  7171 MW;  1BD923A5C0202B99 CRC64;
     MQPVKTVSCP TCGEPAAFSP ENPWRPFCSE RCRMIDLGAW ASESYRIPAK PEESEDEDPP
     VESQ
//
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