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Database: UniProt
Entry: A0A1X9YIZ0_9SPHN
LinkDB: A0A1X9YIZ0_9SPHN
Original site: A0A1X9YIZ0_9SPHN 
ID   A0A1X9YIZ0_9SPHN        Unreviewed;        66 AA.
AC   A0A1X9YIZ0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   ORFNames=KC8_15625 {ECO:0000313|EMBL:ARS28711.1};
OS   Sphingomonas sp. KC8.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS28711.1, ECO:0000313|Proteomes:UP000194475};
RN   [1] {ECO:0000313|EMBL:ARS28711.1, ECO:0000313|Proteomes:UP000194475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC8 {ECO:0000313|EMBL:ARS28711.1};
RA   Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA   Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT   "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT   estrogens in aquatic ecosystems.";
RL   Submitted (JUN-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; CP016306; ARS28711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9YIZ0; -.
DR   KEGG; spkc:KC8_15625; -.
DR   Proteomes; UP000194475; 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   Pfam; PF03884; YacG; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00649};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00649}.
FT   REGION          47..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
FT   BINDING         15
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"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00649"
SQ   SEQUENCE   66 AA;  6928 MW;  BFF44EF4C4DFF789 CRC64;
     MSVPSKRKRG GCPLCGAPAV SAHAPFCSQG CRDRDLLNWL GEAYRTPAAP GDTEAQEIAN
     DGLDTP
//
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