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Database: UniProt
Entry: A0A165QL23_9SPHN
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ID   A0A165QL23_9SPHN        Unreviewed;        62 AA.
AC   A0A165QL23;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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=A3736_01355 {ECO:0000313|EMBL:KZY55987.1};
OS   Erythrobacter sp. HI0063.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY55987.1, ECO:0000313|Proteomes:UP000077326};
RN   [1] {ECO:0000313|EMBL:KZY55987.1, ECO:0000313|Proteomes:UP000077326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0063 {ECO:0000313|EMBL:KZY55987.1,
RC   ECO:0000313|Proteomes:UP000077326};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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}.
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:KZY55987.1}.
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DR   EMBL; LWFF01000274; KZY55987.1; -; Genomic_DNA.
DR   RefSeq; WP_067682029.1; NZ_LWFF01000274.1.
DR   AlphaFoldDB; A0A165QL23; -.
DR   OrthoDB; 9809663at2; -.
DR   Proteomes; UP000077326; 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:UP000077326};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
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   62 AA;  6818 MW;  4AEDC20ACEB2B7F9 CRC64;
     MTNAAKPCPI CRKPRTSEHA PFCSERCRDR DLARWFGDGY AVPGRPALPE EIAAEVTGGQ
     DD
//
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