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Database: UniProt
Entry: A0A2N0X0K5_9GAMM
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Original site: A0A2N0X0K5_9GAMM 
ID   A0A2N0X0K5_9GAMM        Unreviewed;        62 AA.
AC   A0A2N0X0K5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649};
GN   ORFNames=CW745_07515 {ECO:0000313|EMBL:PKF62222.1};
OS   Psychromonas sp. psych-6C06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=2058089 {ECO:0000313|EMBL:PKF62222.1, ECO:0000313|Proteomes:UP000233619};
RN   [1] {ECO:0000313|EMBL:PKF62222.1, ECO:0000313|Proteomes:UP000233619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psych-6C06 {ECO:0000313|Proteomes:UP000233619};
RX   PubMed=27311813; DOI=.1038/ncomms11965;
RA   Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT   "Microbial interactions lead to rapid micro-scale successions on model
RT   marine particles.";
RL   Nat. Commun. 7:11965-11965(2016).
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:PKF62222.1}.
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DR   EMBL; PIZM01000004; PKF62222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0X0K5; -.
DR   OrthoDB; 9809663at2; -.
DR   Proteomes; UP000233619; 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:UP000233619};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00649}.
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="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         24
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"
SQ   SEQUENCE   62 AA;  7258 MW;  2FF336CB57DAA1E6 CRC64;
     MKVNCPTCKK EVEWSKESLH RPFCSKRCQL IDLGEWASEE KRIKGEAVDA ENLPQNKTIY
     FD
//
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