ID A0A3D9BX44_9RHOB Unreviewed; 57 AA.
AC A0A3D9BX44;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN ORFNames=DRV84_05760 {ECO:0000313|EMBL:REC58084.1};
OS Rhodosalinus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC58084.1, ECO:0000313|Proteomes:UP000257131};
RN [1] {ECO:0000313|EMBL:REC58084.1, ECO:0000313|Proteomes:UP000257131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDN1C137 {ECO:0000313|EMBL:REC58084.1,
RC ECO:0000313|Proteomes:UP000257131};
RX PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT saltern.";
RL Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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:REC58084.1}.
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DR EMBL; QOHR01000004; REC58084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9BX44; -.
DR OrthoDB; 9809663at2; -.
DR Proteomes; UP000257131; 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:UP000257131};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ SEQUENCE 57 AA; 6170 MW; C9C5195A13015318 CRC64;
MPCPGCNRPT DPAYRPFCSR RCADVDLARW LSGGYALPGP PLDEEELPPD GPDAPQT
//
