ID A0A0Q4J4Y7_9SPHN Unreviewed; 64 AA.
AC A0A0Q4J4Y7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN ORFNames=ASE85_18415 {ECO:0000313|EMBL:KQN07065.1};
OS Sphingobium sp. Leaf26.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQN07065.1, ECO:0000313|Proteomes:UP000051336};
RN [1] {ECO:0000313|Proteomes:UP000051336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQN07065.1}.
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DR EMBL; LMKV01000005; KQN07065.1; -; Genomic_DNA.
DR RefSeq; WP_056685621.1; NZ_LMKV01000005.1.
DR AlphaFoldDB; A0A0Q4J4Y7; -.
DR STRING; 1735693.ASE85_18415; -.
DR OrthoDB; 9809663at2; -.
DR Proteomes; UP000051336; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="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 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ SEQUENCE 64 AA; 6791 MW; 16D1FE3ABC4F6AB0 CRC64;
MSPKPAACPV CGQPAQAATR PFCSPACRDR DLLQWLGEGY RVPGPAADSD LQKNGNYGLD
SEPD
//